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1. Immunomodulatory Effects of Amblyomma variegatum Saliva on Bovine Cells: Characterization of Cellular Responses and Identification of Molecular Determinants

Author

Valérie Rodrigues, Bernard Fernandez, Arthur Vercoutere, Léo Chamayou, Alexandre Andersen, Oana Vigy, Edith Demettre, Martial Seveno, Rosalie Aprelon, Ken Giraud-Girard, Frédéric Stachurski, Etienne Loire, Nathalie Vachiéry, and Philippe Holzmuller

Subjects
Amblyomma variegatum, tick saliva, PBMC, immuno-modulation, proteomics, Microbiology, QR1-502
Abstract

The tropical bont tick, Amblyomma variegatum, is a tick species of veterinary importance and is considered as one of major pest of ruminants in Africa and in the Caribbean. It causes direct skin lesions, transmits heartwater, and reactivates bovine dermatophilosis. Tick saliva is reported to affect overall host responses through immunomodulatory and anti-inflammatory molecules, among other bioactive molecules. The general objective of this study was to better understand the role of saliva in interaction between the Amblyomma tick and the host using cellular biology approaches and proteomics, and to discuss its impact on disease transmission and/or activation. We first focused on the immuno-modulating effects of semi-fed A. variegatum female saliva on bovine peripheral blood mononuclear cells (PBMC) and monocyte-derived macrophages in vitro. We analyzed its immuno-suppressive properties by measuring the effect of saliva on PBMC proliferation, and observed a significant decrease in ConA-stimulated PBMC lymphoproliferation. We then studied the effect of saliva on bovine macrophages using flow cytometry to analyze the expression of MHC-II and co-stimulation molecules (CD40, CD80, and CD86) and by measuring the production of nitric oxide (NO) and pro- or anti-inflammatory cytokines. We observed a significant decrease in the expression of MHC-II, CD40, and CD80 molecules, associated with decreased levels of IL-12-p40 and TNF-α and increased level of IL-10, which could explain the saliva-induced modulation of NO. To elucidate these immunomodulatory effects, crude saliva proteins were analyzed using proteomics with an Orbitrap Elite mass spectrometer. Among the 336 proteins identified in A. variegatum saliva, we evidenced bioactive molecules exhibiting anti-inflammatory, immuno-modulatory, and anti-oxidant properties (e.g., serpins, phospholipases A2, heme lipoprotein). We also characterized an intriguing ubiquitination complex that could be involved in saliva-induced immune modulation of the host. We propose a model for the interaction between A. variegatum saliva and host immune cells that could have an effect during tick feeding by favoring pathogen dissemination or activation by reducing the efficiency of host immune response to the corresponding tick-borne diseases.

Published
2018
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2. Anopheles gambiae salivary protein expression modulated by wild Plasmodium falciparum infection: highlighting of new antigenic peptides as candidates of An. gambiae bites

Author

Alexandra Marie, Philippe Holzmuller, Majoline T Tchioffo, Marie Rossignol, Edith Demettre, Martial Seveno, Vincent Corbel, Parfait Awono-Ambéné, Isabelle Morlais, Franck Remoue, and Sylvie Cornelie

Subjects
Anopheles gambiae, Wild Plasmodium falciparum, Salivary proteins, Biomarker, Infective bites, Proteomic, Infectious and parasitic diseases, RC109-216
Abstract

Abstract Background Malaria is the major parasitic disease worldwide caused by Plasmodium infection. The objective of integrated malaria control programs is to decrease malaria transmission, which needs specific tools to be accurately assessed. In areas where the transmission is low or has been substantially reduced, new complementary tools have to be developed to improve surveillance. A recent approach, based on the human antibody response to Anopheles salivary proteins, has been shown to be efficient in evaluating human exposure to Anopheles bites. The aim of the present study was to identify new An. gambiae salivary proteins as potential candidate biomarkers of human exposure to P. falciparum-infective bites. Methods Experimental infections of An. gambiae by wild P. falciparum were carried out in semi-field conditions. Then a proteomic approach, combining 2D-DIGE and mass spectrometry, was used to identify the overexpressed salivary proteins in infected salivary glands compared to uninfected An. gambiae controls. Subsequently, a peptide design of each potential candidate was performed in silico and their antigenicity was tested by an epitope-mapping technique using blood from individuals exposed to Anopheles bites. Results Five salivary proteins (gSG6, gSG1b, TRIO, SG5 and long form D7) were overexpressed in the infected salivary glands. Eighteen peptides were designed from these proteins and were found antigenic in children exposed to the Anopheles bites. Moreover, the results showed that the presence of wild P. falciparum in salivary glands modulates the expression of several salivary proteins and also appeared to induce post-translational modifications. Conclusions This study is, to our knowledge, the first that compares the sialome of An. gambiae both infected and not infected by wild P. falciparum, making it possible to mimic the natural conditions of infection. This is a first step toward a better understanding of the close interactions between the parasite and the salivary gland of mosquitoes. In addition, these results open the way to define biomarkers of infective bites of Anopheles, which could, in the future, improve the estimation of malaria transmission and the evaluation of malaria vector control tools.

Published
2014
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3. Trypanosoma cruzi: gene expression surveyed by proteomic analysis reveals interaction between different genotypes in mixed in vitro cultures.

Author

Alexandre Machin, Jenny Telleria, Jean-Paul Brizard, Edith Demettre, Martial Séveno, Francisco José Ayala, and Michel Tibayrenc

Subjects
Medicine, Science
Abstract

We have analyzed the comportment in in vitro culture of 2 different genotypes of Trypanosoma cruzi, the agent of Chagas disease, pertaining to 2 major genetic subdivisions (near-clades) of this parasite. One of the stocks was a fast-growing one, highly virulent in mice, while the other one was slow-growing, mildly virulent in mice. The working hypothesis was that mixtures of genotypes interact, a pattern that has been observed by us in empirical experimental studies. Genotype mixtures were followed every 7 days and characterized by the DIGE technology of proteomic analysis. Proteic spots of interest were characterized by the SAMESPOT software. Patterns were compared to those of pure genotypes that were also evaluated every 7 days. One hundred and three spots exhibited changes in time by comparison with T = 0. The major part of these spots (58%) exhibited an under-expression pattern by comparison with the pure genotypes. 32% of the spots were over-expressed; 10% of spots were not different from those of pure genotypes. Interestingly, interaction started a few minutes after the mixtures were performed. We have retained 43 different proteins that clearly exhibited either under- or over-expression. Proteins showing interaction were characterized by mass spectrometry (MALDI-TOF). Close to 50% of them were either tubulins or heat shock proteins. This study confirms that mixed genotypes of T. cruzi interact at the molecular level. This is of great interest because mixtures of genotypes are very frequent in Chagas natural cycles, both in insect vectors and in mammalian hosts, and may play an important role in the transmission and severity of Chagas disease. The methodology proposed here is potentially applicable to any micropathogen, including fungi, bacteria and viruses. It should be of great interest in the case of bacteria, for which the epidemiological and clinical consequences of mixed infections could be underestimated.

Published
2014
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4. Salivary gland proteome analysis reveals modulation of anopheline unique proteins in insensitive acetylcholinesterase resistant Anopheles gambiae mosquitoes.

Author

Sylvie Cornelie, Marie Rossignol, Martial Seveno, Edith Demettre, François Mouchet, Innocent Djègbè, Philippe Marin, Fabrice Chandre, Vincent Corbel, Franck Remoué, and Françoise Mathieu-Daudé

Subjects
Medicine, Science
Abstract

Insensitive acetylcholinesterase resistance due to a mutation in the acetylcholinesterase (ace) encoding ace-1 gene confers cross-resistance to organophosphate and carbamate insecticides in Anopheles gambiae populations from Central and West Africa. This mutation is associated with a strong genetic cost revealed through alterations of some life history traits but little is known about the physiological and behavioural changes in insects bearing the ace-1(R) allele. Comparative analysis of the salivary gland contents between An. gambiae susceptible and ace-1(R) resistant strains was carried out to charaterize factors that could be involved in modifications of blood meal process, trophic behaviour or pathogen interaction in the insecticide-resistant mosquitoes. Differential analysis of the salivary gland protein profiles revealed differences in abundance for several proteins, two of them showing major differences between the two strains. These two proteins identified as saglin and TRIO are salivary gland-1 related proteins, a family unique to anopheline mosquitoes, one of them playing a crucial role in salivary gland invasion by Plasmodium falciparum sporozoites. Differential expression of two other proteins previously identified in the Anopheles sialome was also observed. The differentially regulated proteins are involved in pathogen invasion, blood feeding process, and protection against oxidation, relevant steps in the outcome of malaria infection. Further functional studies and insect behaviour experiments would confirm the impact of the modification of the sialome composition on blood feeding and pathogen transmission abilities of the resistant mosquitoes. The data supports the hypothesis of alterations linked to insecticide resistance in the biology of the primary vector of human malaria in Africa.

Published
2014
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5. Hijacking of host cellular functions by an intracellular parasite, the microsporidian Anncaliia algerae.

Author

Johan Panek, Hicham El Alaoui, Anne Mone, Serge Urbach, Edith Demettre, Catherine Texier, Christine Brun, Andreas Zanzoni, Eric Peyretaillade, Nicolas Parisot, Emmanuelle Lerat, Pierre Peyret, Frederic Delbac, and David G Biron

Subjects
Medicine, Science
Abstract

Intracellular pathogens including bacteria, viruses and protozoa hijack host cell functions to access nutrients and to bypass cellular defenses and immune responses. These strategies have been acquired through selective pressure and allowed pathogens to reach an appropriate cellular niche for their survival and growth. To get new insights on how parasites hijack host cellular functions, we developed a SILAC (Stable Isotope Labeling by Amino Acids in Cell culture) quantitative proteomics workflow. Our study focused on deciphering the cross-talk in a host-parasite association, involving human foreskin fibroblasts (HFF) and the microsporidia Anncaliia algerae, a fungus related parasite with an obligate intracellular lifestyle and a strong host dependency. The host-parasite cross-talk was analyzed at five post-infection times 1, 6, 12 and 24 hours post-infection (hpi) and 8 days post-infection (dpi). A significant up-regulation of four interferon-induced proteins with tetratricopeptide repeats IFIT1, IFIT2, IFIT3 and MX1 was observed at 8 dpi suggesting a type 1 interferon (IFN) host response. Quantitative alteration of host proteins involved in biological functions such as signaling (STAT1, Ras) and reduction of the translation activity (EIF3) confirmed a host type 1 IFN response. Interestingly, the SILAC approach also allowed the detection of 148 A. algerae proteins during the kinetics of infection. Among these proteins many are involved in parasite proliferation, and an over-representation of putative secreted effectors proteins was observed. Finally our survey also suggests that A. algerae could use a transposable element as a lure strategy to escape the host innate immune system.

Published
2014
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6. Differential expression of salivary proteins between susceptible and insecticide-resistant mosquitoes of Culex quinquefasciatus.

Author

Innocent Djegbe, Sylvie Cornelie, Marie Rossignol, Edith Demettre, Martial Seveno, Franck Remoue, and Vincent Corbel

Subjects
Medicine, Science
Abstract

BACKGROUND: The Culex quinquefasciatus mosquito, a major pest and vector of filariasis and arboviruses in the tropics, has developed multiple resistance mechanisms to the main insecticide classes currently available in public health. Among them, the insensitive acetylcholinesterase (ace-1(R) allele) is widespread worldwide and confers cross-resistance to organophosphates and carbamates. Fortunately, in an insecticide-free environment, this mutation is associated with a severe genetic cost that can affect various life history traits. Salivary proteins are directly involved in human-vector contact during biting and therefore play a key role in pathogen transmission. METHODS AND RESULTS: An original proteomic approach combining 2D-electrophoresis and mass spectrometry was adopted to compare the salivary expression profiles of two strains of C. quinquefasciatus with the same genetic background but carrying either the ace-1(R) resistance allele or not (wild type). Four salivary proteins were differentially expressed (>2 fold, P

Published
2011
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7. Analysis of virion structural components reveals vestiges of the ancestral ichnovirus genome.

Author

Anne-Nathalie Volkoff, Véronique Jouan, Serge Urbach, Sylvie Samain, Max Bergoin, Patrick Wincker, Edith Demettre, François Cousserans, Bertille Provost, Fasseli Coulibaly, Fabrice Legeai, Catherine Béliveau, Michel Cusson, Gabor Gyapay, and Jean-Michel Drezen

Subjects
Immunologic diseases. Allergy, RC581-607, Biology (General), QH301-705.5
Abstract

Many thousands of endoparasitic wasp species are known to inject polydnavirus (PDV) particles into their caterpillar host during oviposition, causing immune and developmental dysfunctions that benefit the wasp larva. PDVs associated with braconid and ichneumonid wasps, bracoviruses and ichnoviruses respectively, both deliver multiple circular dsDNA molecules to the caterpillar. These molecules contain virulence genes but lack core genes typically involved in particle production. This is not completely unexpected given that no PDV replication takes place in the caterpillar. Particle production is confined to the wasp ovary where viral DNAs are generated from proviral copies maintained within the wasp genome. We recently showed that the genes involved in bracovirus particle production reside within the wasp genome and are related to nudiviruses. In the present work we characterized genes involved in ichnovirus particle production by analyzing the components of purified Hyposoter didymator Ichnovirus particles by LC-MS/MS and studying their organization in the wasp genome. Their products are conserved among ichnovirus-associated wasps and constitute a specific set of proteins in the virosphere. Strikingly, these genes are clustered in specialized regions of the wasp genome which are amplified along with proviral DNA during virus particle replication, but are not packaged in the particles. Clearly our results show that ichnoviruses and bracoviruses particles originated from different viral entities, thus providing an example of convergent evolution where two groups of wasps have independently domesticated viruses to deliver genes into their hosts.

Published
2010
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8. First screening ofAedes albopictusimmunogenic salivary proteins

Author

François Favier, Dorothée Missé, François Mouchet, Edith Demettre, Sylvie Cornelie, Martial Séveno, Jean Pierre Hervé, Sirilaksana Patramool, Philippe Gasque, H. Rutee, Jean-Sébastien Dehecq, Souleymane Doucoure, and Franck Remoue

Subjects
Aedes, 0303 health sciences, Saliva, Antigenicity, Aedes albopictus, biology, Protein family, fungi, 030231 tropical medicine, virus diseases, Serpin, biology.organism_classification, Virology, 3. Good health, 03 medical and health sciences, 0302 clinical medicine, Antigen, Insect Science, Genetics, biology.protein, Antibody, Molecular Biology, 030304 developmental biology
Abstract

Study of the human antibody (Ab) response to Aedes salivary proteins can provide new biomarkers to evaluate human exposure to vector bites. The identification of genus- and/or species-specific proteins is necessary to improve the accuracy of biomarkers. We analysed Aedes albopictus immunogenic salivary proteins by 2D immunoproteomic technology and compared the profiles according to human individual exposure to Ae. albopictus or Ae. aegypti bites. Strong antigenicity to Ae. albopictus salivary proteins was detected in all individuals whatever the nature of Aedes exposure. Amongst these antigenic proteins, 68% are involved in blood feeding, including D7 protein family, adenosine deaminase, serpin and apyrase. This study provides an insight into the repertoire of Ae. albopictus immunogenic salivary proteins for the first time.

Published
2013
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9. Proteome ofAedes aegyptiin response to infection and coinfection with microsporidian parasites

Author

Yannis Michalakis, Edith Demettre, Philip Agnew, Alison B. Duncan, Valérie Noël, Martial Séveno, and Jean-Paul Brizard

Subjects
0106 biological sciences, 0303 health sciences, Ecology, biology, Intracellular parasite, Aedes aegypti, biology.organism_classification, medicine.disease, 010603 evolutionary biology, 01 natural sciences, Virology, Plasmodium, 3. Good health, Microbiology, 03 medical and health sciences, Microsporidia, Coinfection, medicine, Parasite hosting, Wolbachia, Pathogen, Ecology, Evolution, Behavior and Systematics, 030304 developmental biology, Nature and Landscape Conservation
Abstract

Hosts are frequently infected with more than one parasite or pathogen at any one time, but little is known as to how they respond to multiple immune challenges compared to those involving single infections. We investigated the proteome of Aedes aegypti larvae following infection with either Edhazardia aedis or Vavraia culicis, and coinfections involving both. They are both obligate intracellular parasites belonging to the phylum microsporidia and infect natural populations of Ae. aegypti. The results found some proteins only showing modified abundance in response to infections involving E. aedis, while others were only differentially abundant when infections involved V. culicis. Some proteins only responded with modified abundance to the coinfection condition, while others were differentially abundant in response to all three types of infection. As time since infection increased, the response to each of the single parasite infections diverged, while the response to the E. aedis and coinfection treatments converged. Some of the proteins differentially abundant in response to infection were identified. They included two vacuolar ATPases, proteins known to have a role in determining the infection success of intracellular parasites. This result suggests microsporidia could influence the infection success of other intracellular pathogens infecting vector species of mosquito, including viruses, Plasmodium and Wolbachia.

Published
2012
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10. Trypanosoma vivax infection in sheep: Different patterns of virulence and pathogenicity associated with differentially expressed proteomes

Author

Jean-Paul Brizard, Álvaro Martínez-Moreno, Armando Reyna-Bello, Martial Séveno, Roger A. Ramírez-Barrios, Lucinda Tavares-Marques, Philippe Holzmuller, Omaira Parra, Robert Valeris, and Edith Demettre

Subjects
Proteomics, Ovin, Protein subunit, Virulence, Parasitemia, L73 - Maladies des animaux, Article, Microbiology, parasitic diseases, medicine, Pathogenicity, L50 - Physiologie et biochimie animales, Marqueur génétique, Trypanosoma vivax, lcsh:Veterinary medicine, General Veterinary, biology, Protéine, General Medicine, Arginine kinase, medicine.disease, biology.organism_classification, Hsp70, biology.protein, lcsh:SF600-1100, Parasitology, HSP60, Biomarkers, Pyruvate kinase
Abstract

Highlights • Trypanosoma vivax strains exhibit different virulence and pathogenicity patterns. • TvMT1 strain showed low virulence and high pathogenicity. • TvLIEM176 strain showed high virulence and moderate pathogenicity. • Protein expression varies in high virulence/moderate pathogenicity strain vs low virulence/high pathogenicity strain., Cattle trypanosomosis caused by Trypanosoma vivax is a widely distributed disease in Africa and Latin America. It causes significant losses in the livestock industry and is characterized by fluctuating parasitemia, anemia, fever, lethargy, and weight loss. In this study we evaluated the virulence (capacity to multiply inside the host and to modulate the host response) and pathogenicity (ability to produce disease and/or mortality) patterns of two T. vivax strains (TvMT1 and TvLIEM176) in experimentally-infected sheep and determined the proteins differentially expressed in the proteomes of these two strains. Hematological and clinical parameters were monitored in experimentally-infected versus non-infected sheep for 60 days. All the infected animals developed discernable parasitemia at 3 days post-infection (dpi), and the first parasitemia peak was observed at 6 dpi. The maximum average value of parasitemia was 1.3 × 107 (95% CI, 7.9 × 105–2 × 108) parasites/ml in TvLIEM176-infected animals, and 2.5 × 106 (95% CI, 1.6 × 105–4 × 107) parasites/ml in TvMT1-infected ones. Anemia and clinical manifestations were more severe in the animals infected by TvMT1 strain than in those infected by TvLIEM176. In the proteomic analysis, a total of 29 proteins were identified, of which 14 exhibited significant differences in their expression levels between strains. Proteins with higher expression in TvLIEM176 were: alpha tubulin, beta tubulin, arginine kinase, glucose-regulated protein 78, paraflagellar protein 3, and T-complex protein 1 subunit theta. Proteins with higher expression in TvMT1 were: chaperonin HSP60, T-complex protein 1 subunit alpha, heat shock protein 70, pyruvate kinase, glycerol kinase, inosine-5'-monophosphate dehydrogenase, 73 kDa paraflagellar rod protein, and vacuolar ATP synthase. There was a difference in the virulence and pathogenicity between the T. vivax strains: TvLIEM176 showed high virulence and moderate pathogenicity, whereas TvMT1 showed low virulence and high pathogenicity. The proteins identified in this study are discussed for their potential involvement in strains’ virulence and pathogenicity, to be further defined as biomarkers of severity in T. vivax infections.

Published
2019
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11. Identification of a Tsal1(52-75) salivary synthetic peptide to monitor cattle exposure to tsetse flies

Author

Sylvie Cornelie, Zakaria Bengaly, Martin Bienvenu Somda, Franck Remoue, Bruno Bucheton, Antoine Sanon, Jeremy Bouyer, Anne Poinsignon, Françoise Mathieu-Daudé, Edith Demettre, Martial Séveno, Emilie Dama, Issa Sidibé, Université Polytechnique Nazi Boni Bobo-Dioulasso (UNB), Centre international de recherche-développement sur l'élevage en zone sub-humide (CIRDES), Vector Control Group (MIVEGEC-VCG), Evolution des Systèmes Vectoriels (ESV), Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Transmission-Interactions-Adaptations hôtes/vecteurs/pathogènes (MIVEGEC-TRIAD), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Contrôle des maladies animales exotiques et émergentes (UMR CMAEE), Institut National de la Recherche Agronomique (INRA)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad), Interactions hôtes-vecteurs-parasites-environnement dans les maladies tropicales négligées dues aux trypanosomatides (UMR INTERTRYP), Université de Bordeaux (UB)-Institut de Recherche pour le Développement (IRD)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad), Projet de Création de Zones Libérées Durablement de Tsé-tsé et de Trypanosomoses (PCZLD), Veterinary Services Department of the Ministry of Food and Agriculture, Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), BioCampus Montpellier (BCM), Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), UFR/SVT, Laboratoire d’Entomologie Fondamentale et Appliquée (LEFA), Université Joseph Ki-Zerbo [Ouagadougou] (UJZK), French Ministry of Foreign Affairs (AIRES-Sud project), 'Institut de Recherche pour le Developpment' (IRD), International Atomic Energy Agency (IAEA), International Foundation for Science (IFS), 'Service de Cooperation et d'Action Culturelle' from the French Embassy in Burkina Faso, Institut de Recherche pour le Développement (IRD [France-Sud])-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut de Recherche pour le Développement (IRD)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université de Bordeaux (UB), Université de Ouagadougou, Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), BioCampus (BCM), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Recherche pour le Développement (IRD)-Université de Bordeaux (UB), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 1 (UM1)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)

Subjects
éradication, Stomoxys, Ectoparasitic Infestations, livestock raising, Epitopes, 0302 clinical medicine, Indicateur biologique, synthetic peptide, bioinformatique, indirect elisa, immunoblotting, African Animal Trypanosomosis, L72 - Organismes nuisibles des animaux, Bétail, Tsetse Flies, Cattle Diseases, Glossina morsitans, tsetse flies, Microbiology, immunoblot analysis, Biodiversity and Ecology, 03 medical and health sciences, Surveillance épidémiologique, Salivary Proteins and Peptides, Test biologique, Linear epitope, Anopheles gambiae, 030104 developmental biology, Parasitology, Immunology, Biomarker of Exposure, Cattle, 0301 basic medicine, Saliva, Identification, glossina, Biodiversité et Ecologie, L73 - Maladies des animaux, biodiversité, antibody, Immunologie, Tabanidae, tsetse fly, 2. Zero hunger, Salive, Amblyomma variegatum, Infectious Diseases, Test ELISA, protéine, african animal trypanosomosis, Peptide, anticorps, biomarker of exposure, Trypanosoma, 030231 tropical medicine, Enzyme-Linked Immunosorbent Assay, Biology, betail, cattle, composition de la salive, Synthetic Peptide, Animals, technique elisa, Bovin, Research, Technique immunologique, Tsetse fly, mouche tsé tsé, biology.organism_classification, Immunoglobulin G, U30 - Méthodes de recherche, [SDE.BE]Environmental Sciences/Biodiversity and Ecology, protein
Abstract

Background The saliva of tsetse flies contains a cocktail of bioactive molecules inducing specific antibody responses in hosts exposed to bites. We have previously shown that an indirect-ELISA test using whole salivary extracts from Glossina morsitans submorsitans was able to discriminate between (i) cattle from tsetse infested and tsetse free areas and (ii) animals experimentally exposed to low or high numbers of tsetse flies. In the present study, our aim was to identify specific salivary synthetic peptides that could be used to develop simple immunoassays to measure cattle exposure to tsetse flies. Methods In a first step, 2D-electrophoresis immunoblotting, using sera from animals exposed to a variety of bloodsucking arthropods, was performed to identify specific salivary proteins recognised in cattle exposed to tsetse bites. Linear epitope prediction software and Blast analysis were then used to design synthetic peptides within the identified salivary proteins. Finally, candidate peptides were tested by indirect-ELISA on serum samples from tsetse infested and tsetse free areas, and from exposure experiments. Results The combined immunoblotting and bioinformatics analyses led to the identification of five peptides carrying putative linear epitopes within two salivary proteins: the tsetse salivary gland protein 1 (Tsal1) and the Salivary Secreted Adenosine (SSA). Of these, two were synthesised and tested further based on the absence of sequence homology with other arthropods or pathogen species. IgG responses to the Tsal152–75 synthetic peptide were shown to be specific of tsetse exposure in both naturally and experimentally exposed hosts. Nevertheless, anti-Tsal152–75 IgG responses were absent in animals exposed to high tsetse biting rates. Conclusions These results suggest that Tsal152–75 specific antibodies represent a biomarker of low cattle exposure to tsetse fly. These results are discussed in the light of the other available tsetse saliva based-immunoassays and in the perspective of developing a simple serological tool for tsetse eradication campaigns to assess the tsetse free status or to detect tsetse reemergence in previously cleared areas. Electronic supplementary material The online version of this article (doi:10.1186/s13071-016-1414-8) contains supplementary material, which is available to authorized users.

Published
2016
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12. The proteomic analysis of mouse choroid plexus secretome reveals a high protein secretion capacity of choroidal epithelial cells

Author

Eric Thouvenot, Joël Bockaert, Mireille Lafon-Cazal, Edith Demettre, Philippe Marin, and Patrick Jouin

Subjects
Lipopolysaccharides, Proteomics, Proteases, Proteins, Epithelial Cells, Fibroblasts, Biology, Biochemistry, Molecular biology, Cell biology, Transport protein, Extracellular matrix, Mice, Secretory protein, Cerebrospinal fluid, Astrocytes, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Choroid Plexus, cardiovascular system, Animals, Secretion, Choroid plexus, Molecular Biology, Cells, Cultured
Abstract

Choroid plexuses (CP) are involved in multiple functions related to their unique architecture and localization at the interface between the blood and cerebrospinal fluid compartments. These include the release by choroidal epithelial cells (CEC) of biologically active molecules, such as polypeptides, which are distributed globally to the brain. Here, we have used a proteomic approach to get an unbiased overview of the proteins that are secreted by primary cultures enriched in epithelial cells from mice CP. We identified a total of 43 proteins secreted through the classical vesicular pathway in CEC -conditioned medium. They include transport proteins, collagen subunits and other cell matrix proteins, proteases, protease inhibitors and neurotrophic factors. Treating CEC cultures with lipopolysaccharide, increased the secretion of four protein species and induced the release of two additional proteins. Our study also reveals a higher protein secretion capacity of CECs compared with other CP cells or cultured astrocytes. In conclusion, this study provides for the first time the characterization of the major proteins that are secreted by CECs. These proteins may play a critical role in neuronal growth, differentiation and function as well as in brain pathologies.

Published
2006
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13. Proteomic detection of prostate-specific antigen using a serum fractionation procedure: potential implication for new low-abundance cancer biomarkers detection

Author

Thierry Maudelonde, Edith Demettre, Jérôme Solassol, Alain Mangé, Philippe Rouanet, Joël Bockaert, and Philippe Marin

Subjects
Proteomics, Chemistry, Biophysics, Albumin, Cell Biology, Fractionation, Chemical Fractionation, Prostate-Specific Antigen, medicine.disease, Biochemistry, Molecular biology, Mass Spectrometry, Ion Exchange, Prostate-specific antigen, Prostate cancer, Antigen, medicine, Animals, Electrophoresis, Polyacrylamide Gel, Cancer biomarkers, Molecular Biology, Biomarkers, Tumor marker
Abstract

One of the major obstacles in proteomic analysis of biological fluids is the presence of highly abundant proteins such as albumin and immunoglobulins, which can interfere with the resolution and sensitivity of the proteome profiling techniques used. In this paper, we describe an anion exchange fractionation procedure for serum using denaturating conditions allowing protein-protein interaction disruption before analysis by surface-enhanced laser desorption/ionization and by two-dimensional electrophoresis. This method simplifies the serum proteome into subproteomes and markedly increases resolution and sensitivity without any loss of minor proteins. To confirm the applicability of this method, fractionated serum of a patient with prostate cancer was analyzed for the presence of the prostate-specific antigen (PSA) which is a low-abundance tumor marker protein. The results demonstrate that PSA can be detected by two-dimensional electrophoresis only in serum following fractionation. Hence, this procedure may facilitate the identification of other, so far unknown, tumor markers in patient sera.

Published
2005
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14. Recurrent DNA virus domestication leading to different parasite virulence strategies

Author

Serge Urbach, Annie Bézier, Vonick Sibut, Julien Thézé, Sandra Schmieder, Anne-Nathalie Volkoff, Marylène Poirié, Marc Ravallec, Valérie Barbe, François Cousserans, Apolline Pichon, Edith Demettre, Dominique Colinet, Arnaud Couloux, Jean-Marc Aury, Jérémy Gauthier, Jean-Michel Drezen, Julie Guy, Corinne Da Silva, François Wurmser, Véronique Jouan, Institutions et Dynamiques Historiques de l'Économie et de la Société (IDHES), Ecole Normale Supérieure Paris-Saclay (ENS Paris Saclay)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Nanterre (UPN)-Université Paris 8 Vincennes-Saint-Denis (UP8)-Université Paris 1 Panthéon-Sorbonne (UP1), Université d'Évry-Val-d'Essonne (UEVE), Institut de recherche sur la biologie de l'insecte UMR7261 (IRBI), Université de Tours-Centre National de la Recherche Scientifique (CNRS), Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), BioCampus Montpellier (BCM), Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'Energie Atomique, Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Diversité, Génomes & Interactions Microorganismes - Insectes [Montpellier] (DGIMI), Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Recherche Agronomique (INRA), Centre de Recherches sur les Économies, les Sociétés, les Arts et les Techniques (CRESAT), Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA)), Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Evolution, Génomes et Spéciation (LEGS), Centre National de la Recherche Scientifique (CNRS), Institut Sophia Agrobiotech (ISA), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Recherche Agronomique (INRA), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Génomique métabolique (UMR 8030), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE), Genoscope French National Research Agency (ANR) Appeared in article as French National Research Agency ANR-09-BLAN-0243-01, ANR-09-BLAN-0243,PARATOXOSE(2009), École normale supérieure - Cachan (ENS Cachan)-Université Panthéon-Sorbonne (UP1)-Université Paris 8 Vincennes-Saint-Denis (UP8)-Université Paris Nanterre (UPN)-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 1 (UM1)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), UPR9034, Laboratoire Évolution Génomes et Spéciation, Université Paris Sud (Paris 11)-Centre National de la Recherche Scientifique (CNRS), Institut Sophia Agrobiotech [Sophia Antipolis] (ISA), Institut National de la Recherche Agronomique (INRA)-Université Nice Sophia Antipolis (... - 2019) (UNS), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE), Université Paris 1 Panthéon-Sorbonne (UP1)-Université Paris 8 Vincennes-Saint-Denis (UP8)-Université Paris Nanterre (UPN)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS)-Ecole Normale Supérieure Paris-Saclay (ENS Paris Saclay), Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), BioCampus (BCM), Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM), Université Nice Sophia Antipolis (1965 - 2019) (UNS), Institut National de la Recherche Agronomique (INRA)-Université Nice Sophia Antipolis (1965 - 2019) (UNS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure - Cachan (ENS Cachan)-Université Panthéon-Sorbonne (UP1)-Université Paris 8 Vincennes-Saint-Denis (UP8)-Université Paris Nanterre (UPN)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Belloufi, Aicha, Blanc - - PARATOXOSE2009 - ANR-09-BLAN-0243 - Blanc - VALID, Drezen, Jean-Michel, and Volkoff, Anne Nathalie

Subjects
Microscope Electronique à Transmission, 0106 biological sciences, hôte, Biodiversité et Ecologie, viruses, Virulence, virus, macromolecular substances, 010603 evolutionary biology, 01 natural sciences, Genome, Microbiology, Virus, Biodiversity and Ecology, Nudivirus, 03 medical and health sciences, virus domestication, [SDV.BID.EVO] Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE], guêpe, Domestication, Research Articles, 030304 developmental biology, [SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology, Genetics, 0303 health sciences, Multidisciplinary, biology, Host (biology), gène viral, [SDV.BID.EVO]Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE], fungi, eucaryote, SciAdv r-articles, Life Sciences, DNA virus, venturia canescens, wasps, biology.organism_classification, 3. Good health, [SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate Zoology, liposome, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, [SDV.BA.ZI] Life Sciences [q-bio]/Animal biology/Invertebrate Zoology, Eukaryote, séquençage adn, genomes, Research Article
Abstract

Virus domestication is a recurrent and beneficial process in the evolution of parasitic wasps., Relics of ancient infections are abundant in eukaryote genomes, but little is known about how they evolve when they confer a functional benefit on their host. We show here, for the first time, that the virus-like particles shown to protect Venturia canescens eggs against host immunity are derived from a nudivirus genome incorporated by the parasitic wasp into its own genetic material. Nudivirus hijacking was also at the origin of protective particles from braconid wasps. However, we show here that the viral genes produce “liposomes” that wrap and deliver V. canescens virulence proteins, whereas the particles are used as gene transfer agents in braconid wasps. Our findings indicate that virus domestication has occurred repeatedly during parasitic wasp evolution but with different evolutionary trajectories after endogenization, resulting in different virulence molecule delivery strategies.

Published
2015
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15. Ribonuclease L Proteolysis in Peripheral Blood Mononuclear Cells of Chronic Fatigue Syndrome Patients

Author

Patrick Englebienne, Bernard Lebleu, A. D'haese, L. Bastide, Kenny De Meirleir, Edith Demettre, Kiet Tiev, and Karen De Smet

Subjects
Proteases, RNase P, Proteolysis, Biology, Biochemistry, Peripheral blood mononuclear cell, Monocytes, law.invention, Ribonucleases, law, 2',5'-Oligoadenylate Synthetase, medicine, Humans, Binding site, Molecular Biology, Nuclease, Fatigue Syndrome, Chronic, medicine.diagnostic_test, Hydrolysis, Cell Biology, Molecular biology, Recombinant Proteins, Recombinant DNA, biology.protein, Ribonuclease L
Abstract

A 37-kDa binding polypeptide accumulates in peripheral blood mononuclear cell (PBMC) extracts from chronic fatigue syndrome (CFS) patients and is being considered as a potential diagnostic marker (De Meirleir, K., Bisbal, C., Campine, I., De Becker, P., Salehzada, T., Demettre, E., and Lebleu, B. (2000) Am. J. Med. 108, 99-105). We establish here that this low molecular weight 2-5A-binding polypeptide is a truncated form of the native 2-5A-dependent ribonuclease L (RNase L), generated by an increased proteolytic activity in CFS PBMC extracts. RNase L proteolysis in CFS PBMC extracts can be mimicked in a model system in which recombinant RNase L is treated with human leukocyte elastase. RNase L proteolysis leads to the accumulation of two major fragments with molecular masses of 37 and 30 kDa. The 37-kDa fragment includes the 2-5A binding site and the N-terminal end of native RNase L. The 30-kDa fragment includes the catalytic site in the C-terminal part of RNase L. Interestingly, RNase L remains active and 2-5A-dependent when degraded into its 30- and 37-kDa fragments by proteases of CFS PBMC extract or by purified human leukocyte elastase. The 2-5A-dependent nuclease activity of the truncated RNase L could result from the association of these digestion products, as suggested in pull down experiments.

Published
2002
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16. Anopheles gambiae salivary protein expression modulated by wild Plasmodium falciparum infection : highlighting of new antigenic peptides as candidates of An. gambiae bites

Author

Marie-Noëlle Rossignol, Isabelle Morlais, Franck Remoue, Alexandra Marie, Edith Demettre, Vincent Corbel, Martial Séveno, Parfait Awono-Ambene, Philippe Holzmuller, Sylvie Cornelie, Majoline T. Tchioffo, Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Institut de Recherche pour le Développement (IRD [France-Sud])-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Contrôle des maladies animales exotiques et émergentes (UMR CMAEE), Institut National de la Recherche Agronomique (INRA)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad), Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Vector Control Group (MIVEGEC-VCG), Evolution des Systèmes Vectoriels (ESV), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Centre National de la Recherche Scientifique (CNRS)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 1 (UM1)-Université de Montpellier (UM), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA), and Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Male, Infective bites, Anopheles gambiae, [SDV]Life Sciences [q-bio], L73 - Maladies des animaux, Plasmodium, Salivary Glands, 0302 clinical medicine, Malaria, Falciparum, proteomic, 0303 health sciences, biology, Salivary gland, Anopheles, 3. Good health, medicine.anatomical_structure, Infectious Diseases, infective bites, Sialome, Parasitic disease, Insect Proteins, Female, L72 - Organismes nuisibles des animaux, 030231 tropical medicine, Plasmodium falciparum, 03 medical and health sciences, parasitic diseases, medicine, Animals, Humans, Wild plasmodium falciparum, Wild Plasmodium falciparum, [SDV.MP.PAR]Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology, Salivary Proteins and Peptides, 030304 developmental biology, [SDV.GEN.GPO]Life Sciences [q-bio]/Genetics/Populations and Evolution [q-bio.PE], Research, Proteomic, Insect Bites and Stings, Biomarker, Salivary Proteins, medicine.disease, biology.organism_classification, Salivary proteins, Virology, Parasitology, Malaria, Biomarkers
Abstract

Background Malaria is the major parasitic disease worldwide caused by Plasmodium infection. The objective of integrated malaria control programs is to decrease malaria transmission, which needs specific tools to be accurately assessed. In areas where the transmission is low or has been substantially reduced, new complementary tools have to be developed to improve surveillance. A recent approach, based on the human antibody response to Anopheles salivary proteins, has been shown to be efficient in evaluating human exposure to Anopheles bites. The aim of the present study was to identify new An. gambiae salivary proteins as potential candidate biomarkers of human exposure to P. falciparum-infective bites. Methods Experimental infections of An. gambiae by wild P. falciparum were carried out in semi-field conditions. Then a proteomic approach, combining 2D-DIGE and mass spectrometry, was used to identify the overexpressed salivary proteins in infected salivary glands compared to uninfected An. gambiae controls. Subsequently, a peptide design of each potential candidate was performed in silico and their antigenicity was tested by an epitope-mapping technique using blood from individuals exposed to Anopheles bites. Results Five salivary proteins (gSG6, gSG1b, TRIO, SG5 and long form D7) were overexpressed in the infected salivary glands. Eighteen peptides were designed from these proteins and were found antigenic in children exposed to the Anopheles bites. Moreover, the results showed that the presence of wild P. falciparum in salivary glands modulates the expression of several salivary proteins and also appeared to induce post-translational modifications. Conclusions This study is, to our knowledge, the first that compares the sialome of An. gambiae both infected and not infected by wild P. falciparum, making it possible to mimic the natural conditions of infection. This is a first step toward a better understanding of the close interactions between the parasite and the salivary gland of mosquitoes. In addition, these results open the way to define biomarkers of infective bites of Anopheles, which could, in the future, improve the estimation of malaria transmission and the evaluation of malaria vector control tools. Electronic supplementary material The online version of this article (doi:10.1186/s13071-014-0599-y) contains supplementary material, which is available to authorized users.

Published
2014
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17. Hijacking of Host Cellular Functions by an Intracellular Parasite, the Microsporidian Anncaliia algerae

Author

Eric Peyretaillade, Hicham El Alaoui, Frédéric Delbac, Johan Panek, Edith Demettre, Nicolas Parisot, Andreas Zanzoni, David Biron, Catherine Texier, Pierre Peyret, Serge Urbach, Emmanuelle Lerat, Anne Moné, Christine Brun, Laboratoire Microorganismes : Génome et Environnement (LMGE), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Centre National de la Recherche Scientifique (CNRS), Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Technologies avancées pour le génôme et la clinique (TAGC), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Conception, Ingénierie et Développement de l'Aliment et du Médicament (CIDAM), Université d'Auvergne - Clermont-Ferrand I (UdA), Eléments transposables, évolution, populations, Département génétique, interactions et évolution des génomes [LBBE] (GINSENG), Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Moné, Anne

Subjects
Proteomics, Proteome, Host cells, [SDV]Life Sciences [q-bio], Intracellular Space, lcsh:Medicine, Pathogenesis, Pathology and Laboratory Medicine, Biochemistry, SILAC, 0302 clinical medicine, Interferon, Stable isotope labeling by amino acids in cell culture, Medicine and Health Sciences, lcsh:Science, Hypoxia, [INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM], Fungal Pathogens, 0303 health sciences, Fungal protein, Multidisciplinary, [SDV.BIBS] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Effector, Parasitic diseases, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Cell biology, [SDV] Life Sciences [q-bio], Medical Microbiology, Intracellular parasite, Research Article, medicine.drug, Biology, Microbiology, microsporidia Anncaliia algerae, Host-Parasite Interactions, Fungal Proteins, 03 medical and health sciences, Anncaliia algerae, medicine, Humans, Immune response, Microbial Pathogens, 030304 developmental biology, Intracellular pathogens, Innate immune system, Host-pathogen interactions, lcsh:R, Biology and Life Sciences, Fibroblasts, Microsporidia, DNA Transposable Elements, Parasitology, lcsh:Q, Interferons, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM], 030217 neurology & neurosurgery
Abstract

International audience; Intracellular pathogens including bacteria, viruses and protozoa hijack host cell functions to access nutrients and to bypass cellular defenses and immune responses. These strategies have been acquired through selective pressure and allowed pathogens to reach an appropriate cellular niche for their survival and growth. To get new insights on how parasites hijack host cellular functions, we developed a SILAC (Stable Isotope Labeling by Amino Acids in Cell culture) quantitative proteomics workflow. Our study focused on deciphering the cross-talk in a host-parasite association, involving human foreskin fibroblasts (HFF) and the microsporidia Anncaliia algerae, a fungus related parasite with an obligate intracellular lifestyle and a strong host dependency. The host-parasite cross-talk was analyzed at five post-infection times 1, 6, 12 and 24 hours post-infection (hpi) and 8 days post-infection (dpi). A significant up-regulation of four interferon-induced proteins with tetratricopeptide repeats IFIT1, IFIT2, IFIT3 and MX1 was observed at 8 dpi suggesting a type 1 interferon (IFN) host response. Quantitative alteration of host proteins involved in biological functions such as signaling (STAT1, Ras) and reduction of the translation activity (EIF3) confirmed a host type 1 IFN response. Interestingly, the SILAC approach also allowed the detection of 148 A. algerae proteins during the kinetics of infection. Among these proteins many are involved in parasite proliferation, and an over-representation of putative secreted effectors proteins was observed. Finally our survey also suggests that A. algerae could use a transposable element as a lure strategy to escape the host innate immune system.

Published
2014
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18. Trypanosoma cruzi : gene expression surveyed by proteomic analysis reveals interaction between different genotypes in mixed in vitro cultures

Author

Francisco J. Ayala, Michel Tibayrenc, Jenny Telleria, Edith Demettre, Alexandre Machin, Jean-Paul Brizard, and Martial Séveno

Subjects
Proteomics, Evolutionary Genetics, Proteome, lcsh:Medicine, Biochemistry, 0302 clinical medicine, Genotype, Medicine and Health Sciences, Parasite hosting, lcsh:Science, Genetics, 0303 health sciences, Multidisciplinary, Genomics, 3. Good health, Infectious Diseases, Transcriptome Analysis, Sequence Analysis, Research Article, Chagas disease, Trypanosoma cruzi, 030231 tropical medicine, DNA transcription, Virulence, Biology, Microbiology, 03 medical and health sciences, Heat shock protein, medicine, Parasitic Diseases, Chagas Disease, Parasite Evolution, Molecular Biology Techniques, Sequencing Techniques, Molecular Biology, 030304 developmental biology, Evolutionary Biology, Protozoan Infections, Biology and life sciences, lcsh:R, Computational Biology, biology.organism_classification, Leishmania, medicine.disease, Genome Analysis, lcsh:Q, Parasitology, Gene expression, Genome Expression Analysis, Transcriptome
Abstract

We have analyzed the comportment in in vitro culture of 2 different genotypes of Trypanosoma cruzi, the agent of Chagas disease, pertaining to 2 major genetic subdivisions (near-clades) of this parasite. One of the stocks was a fast-growing one, highly virulent in mice, while the other one was slow- growing, mildly virulent in mice. The working hypothesis was that mixtures of genotypes interact, a pattern that has been observed by us in empirical experimental studies. Genotype mixtures were followed every 7 days and characterized by the DIGE technology of proteomic analysis. Proteic spots of interest were characterized by the SAMESPOT software. Patterns were compared to those of pure genotypes that were also evaluated every 7 days. One hundred and three spots exhibited changes in time by comparison with T = 0. The major part of these spots (58%) exhibited an under-expression pattern by comparison with the pure genotypes. 32% of the spots wereover-expressed; 10% of spots were not different from those of pure genotypes. Interestingly, interaction started a few minutes after the mixtures were performed. We have retained 43 different proteins that clearly exhibited either under- or over-expression. Proteins showing interaction were characterized by mass spectrometry (MALDI-TOF). Close to 50% of them were either tubulins or heat shock proteins. This study confirms that mixed genotypes of T. cruzi interact at the molecular level. This is of great interest because mixtures of genotypes are very frequent in Chagas natural cycles, both in insect vectors and in mammalian hosts, and may play an important role in the transmission and severity of Chagas disease. The methodology proposed here is potentially applicable to any micropathogen, including fungi, bacteria and viruses. It should be of great interest in the case of bacteria, for which the epidemiological and clinical consequences of mixed infections could be underestimated.

Published
2014

19. Salivary gland proteome analysis reveals modulation of anopheline unique proteins in insensitive acetylcholinesterase resistant Anopheles gambiae mosquitoes

Author

Franck Remoue, Fabrice Chandre, Sylvie Cornelie, Françoise Mathieu-Daudé, Marie Rossignol, Philippe Marin, Martial Séveno, Vincent Corbel, Innocent Djègbè, Edith Demettre, François Mouchet, Vector Control Group (MIVEGEC-VCG), Evolution des Systèmes Vectoriels (ESV), Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Centre National de la Recherche Scientifique (CNRS)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 1 (UM1)-Université de Montpellier (UM), and Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Proteomics, Proteome, Epidemiology, Anopheles gambiae, Plasmodium falciparum/physiology, Disease Vectors, Biochemistry, Mosquitoes, Salivary Glands, Insect Proteins/chemistry/isolation & purification, Insecticide Resistance, Medicine and Health Sciences, Pathogen, Genetics, Principal Component Analysis, Multidisciplinary, Spectrometric Identification of Proteins, biology, Salivary gland, Anopheles, 3. Good health, Insects, Anopheles gambiae/genetics/*metabolism/parasitology, medicine.anatomical_structure, Sialome, Insecticide Resistance/*genetics, Acetylcholinesterase, Insect Proteins, Medicine, Sequence Analysis, Research Article, Arthropoda, Science, Plasmodium falciparum, Microbiology, Vector Biology, Host-Parasite Interactions, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], parasitic diseases, medicine, Animals, Matrix-Assisted Laser Desorption-Ionization, Molecular Biology Techniques, Sequencing Techniques, Molecular Biology, Spectrometry, Organisms, Biology and Life Sciences, Salivary Glands/metabolism, Mass, biology.organism_classification, Molecular biology, Invertebrates, [SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate Zoology, Acetylcholinesterase/*genetics, Vector (epidemiology), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Parasitology, Gene Function, Zoology, Entomology, Protein Abundance
Abstract

International audience; Insensitive acetylcholinesterase resistance due to a mutation in the acetylcholinesterase (ace) encoding ace-1 gene confers cross-resistance to organophosphate and carbamate insecticides in Anopheles gambiae populations from Central and West Africa. This mutation is associated with a strong genetic cost revealed through alterations of some life history traits but little is known about the physiological and behavioural changes in insects bearing the ace-1(R) allele. Comparative analysis of the salivary gland contents between An. gambiae susceptible and ace-1(R) resistant strains was carried out to charaterize factors that could be involved in modifications of blood meal process, trophic behaviour or pathogen interaction in the insecticide-resistant mosquitoes. Differential analysis of the salivary gland protein profiles revealed differences in abundance for several proteins, two of them showing major differences between the two strains. These two proteins identified as saglin and TRIO are salivary gland-1 related proteins, a family unique to anopheline mosquitoes, one of them playing a crucial role in salivary gland invasion by Plasmodium falciparum sporozoites. Differential expression of two other proteins previously identified in the Anopheles sialome was also observed. The differentially regulated proteins are involved in pathogen invasion, blood feeding process, and protection against oxidation, relevant steps in the outcome of malaria infection. Further functional studies and insect behaviour experiments would confirm the impact of the modification of the sialome composition on blood feeding and pathogen transmission abilities of the resistant mosquitoes. The data supports the hypothesis of alterations linked to insecticide resistance in the biology of the primary vector of human malaria in Africa.

Published
2014
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20. New Export Pathway in Plasmodium falciparum-Infected Erythrocytes: Role of the Parasite Group II Chaperonin, PfTRiC

Author

Alassane, Mbengue, Emilie, Vialla, Laurence, Berry, Gamou, Fall, Nicolas, Audiger, Edith, Demettre-Verceil, David, Boteller, and Catherine, Braun-Breton

Subjects
Cytoplasm, Protein Transport, Erythrocytes, Merozoites, Erythrocyte Membrane, Plasmodium falciparum, Group II Chaperonins, Protozoan Proteins, Humans, Cells, Cultured, Host-Parasite Interactions
Abstract

The export of numerous proteins to the plasma membrane of its host erythrocyte is essential for the virulence and survival of the malaria parasite Plasmodium falciparum. The Maurer's clefts, membrane structures transposed by the parasite in the cytoplasm of its host erythrocyte, play the role of a marshal platform for such exported parasite proteins. We identify here the export pathway of three resident proteins of the Maurer's clefts membrane: the proteins are exported as soluble forms in the red cell cytoplasm to the Maurer's clefts membrane in association with the parasite group II chaperonin (PfTRIC), a chaperone complex known to bind and address a large spectrum of unfolded proteins to their final location. We have also located the domain of interaction with PfTRiC within the amino-terminal domain of one of these Maurer's cleft proteins, PfSBP1. Because several Maurer's cleft membrane proteins with different export motifs seem to follow the same route, we propose a general role for PfTRiC in the trafficking of malarial parasite proteins to the host erythrocyte.

Published
2013

21. Identification of Glossina palpalis gambiensis specific salivary antigens: towards the development of a serologic biomarker of human exposure to tsetse flies in West Africa

Author

Martial Séveno, Franck Remoue, Fabrice Courtin, Zakaria Bengaly, Vincent Jamonneau, Mamadou Camara, Anne Poinsignon, Philippe Solano, R. Kambiré, Edith Demettre, Martin Bienvenu Somda, Adrien Marie Gaston Belem, Sylvie Cornelie, Bruno Bucheton, Emilie Dama, Transmission-Interactions-Adaptations hôtes/vecteurs/pathogènes (MIVEGEC-TRIAD), Evolution des Systèmes Vectoriels (ESV), Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Institut de Recherche pour le Développement (IRD [France-Sud])-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut de Recherche pour le Développement (IRD [France-Sud])-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Institut de Recherche pour le Développement (IRD [France-Sud])-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut de Recherche pour le Développement (IRD [France-Sud])-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), and Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])

Subjects
Male, Saliva, Disease Vectors, Immunoglobulin G, Mass Spectrometry, Salivary Glands, Serology, 0302 clinical medicine, African trypanosomiasis, Electrophoresis, Gel, Two-Dimensional, Child, ComputingMilieux_MISCELLANEOUS, Aged, 80 and over, Human African trypanosomosis, 0303 health sciences, Glossina saliva, Middle Aged, 3. Good health, Infectious Diseases, Child, Preschool, Insect Proteins, Female, Antibody, Adult, Adolescent, Tsetse Flies, 030231 tropical medicine, Immunology, Enzyme-Linked Immunosorbent Assay, Biology, Microbiology, Insect bites and stings, Antibodies, Exposure, 03 medical and health sciences, Young Adult, Antigen, parasitic diseases, Burkina Faso, medicine, Animals, Humans, Salivary Proteins and Peptides, 030304 developmental biology, Aged, Insect Bites and Stings, Biomarker, medicine.disease, Virology, Vector (epidemiology), biology.protein, Guinea, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology, Biomarkers
Abstract

The saliva of blood sucking arthropods contains a number of pharmacologically active compounds that induce an antibody response in exposed human individuals. The objectives of the present study were (i) to assess the human IgG response directed against salivary antigens of Glossina palpalis gambiensis, the main vector of Trypanosoma brucei gambiense in West Africa, as a biomarker of human tsetse contacts; and (ii) to identify specific salivary antigens. Immune reactivity of human plasma collected within active human African trypanosomiasis (HAT) foci (coastal Guinea), historical foci where tsetse flies are still present (South-West Burkina Faso) and a tsetse free area (Bobo-Dioulasso, Burkina Faso), was measured by ELISA against whole saliva extracts. In the active HAT foci and areas where tsetse flies were present in high densities, specific IgG responses were significantly higher (p < 0.0001) to those in Bobo-Dioulasso or in Loropeni, where tsetse flies were either absent or only present at low densities. Furthermore, 2D-electrophoresis combined with mass spectrometry enabled to reveal that several antigens were specifically recognized by plasma from exposed individuals. Among them, four salivary proteins were successfully identified (Ada, 5'Nuc, Ag5 and Tsgf1). These results represent a first attempt to identify Glossina salivary proteins or synthetic peptides to develop a standardized and specific biomarker of tsetse exposure in West Africa.

Published
2013
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22. Venom gland extract is not required for successful parasitism in the polydnavirus-associated endoparasitoid Hyposoter didymator (Hym. Ichneumonidae) despite the presence of numerous novel and conserved venom proteins

Author

Eric Wajnberg, Tristan Dorémus, Jean-Luc Gatti, Serge Urbach, Véronique Jouan, Dominique Colinet, Anne-Nathalie Volkoff, Marylène Poirié, Carole Azéma-Dossat, Julie Poulain, François Cousserans, Edith Demettre, Isabelle Darboux, Marc Ravallec, Jean-Michel Escoubas, Diversité, Génomes & Interactions Microorganismes - Insectes [Montpellier] (DGIMI), Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM), Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Institut Sophia Agrobiotech [Sophia Antipolis] (ISA), Institut National de la Recherche Agronomique (INRA)-Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), UMR 7254, Centre National de la Recherche Scientifique (CNRS), IG, Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Genoscope ('Parasitoid venoms' project), French National Research Agency (Paratoxose project) [ANR-09-BLAN-0243-01], Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Recherche Agronomique (INRA), Institut Sophia Agrobiotech (ISA), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Recherche Agronomique (INRA), ANR-09-BLAN-0243,PARATOXOSE(2009), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Université Nice Sophia Antipolis (1965 - 2019) (UNS), and COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Male, 0106 biological sciences, Proteomics, Cellular immunity, Proteome, Hydrolases, [SDV]Life Sciences [q-bio], Wasps, Wasp Venoms, Venom, 01 natural sciences, Biochemistry, Polydnavirus, Ichneumonid, Immunity, Cellular, 0303 health sciences, Microscopy, biology, Spodoptera frugiperda, 3. Good health, Larva, Insect immunity, Insect Proteins, Female, Serine Proteinase Inhibitors, Molecular Sequence Data, Hyposoter didymator, Spodoptera, Serpin, 010603 evolutionary biology, complex mixtures, Host-Parasite Interactions, 03 medical and health sciences, Exocrine Glands, Botany, Animals, Amino Acid Sequence, Molecular Biology, 030304 developmental biology, Gene Expression Profiling, Sequence Analysis, DNA, Venom Protein, biology.organism_classification, Hymenoptera, Parasitoid, Insect Science, Campopleginae, Host regulation, Transcriptome, Parasitism success
Abstract

Corrigendum to “Venom gland extract is not required for successful parasitism in the polydnavirus-associated endoparasitoid Hyposoter didymator (Hym. Ichneumonidae) despite the presence of numerous novel and conserved venom proteins” [Insect Biochem. Mol. Biol. 43 (2013), 292–307] http://dx.doi.org/10.1016/j.ibmb.2013.07.001(UT:000329772300006); The venom gland is a conserved organ in Hymenoptera that shows adaptations associated with life-style diversification. Few studies have investigated venom components and function in the highly diverse parasitic wasps and all suggest that the venom regulates host physiology. We explored the venom of the endoparasitoid Hyposoter didymator (Campopleginae), a species with an associated polydnavirus produced in the ovarian tissue. We investigated the effects of the H. didymator venom on two physiological traits of the host Spodoptera frugiperda (Noctuidae): encapsulation response and growth rate. We found that H. didymator venom had no significant effect on host cellular immunity or development, suggesting that it does not contribute to parasitism success. The host physiology seemed to be modified essentially by the ovarian fluid containing the symbiotic polydnaviruses. Proteomic analyses indicated that the H. didymator venom gland produces a large variety of proteins, consistent with the classical hymenopteran venom protein signature, including: reprolysin-like, dipeptidyl peptidase IV, hyaluronidase, arginine kinase or allergen proteins. The venom extracts also contained novel proteins, encoded by venom genes conserved in Campopleginae ichneumonids, and proteins with similarities to active molecules identified in other parasitoid species, such as calreticulin, reprolysin, superoxide dismutase and serpin. However, some of these proteins appear to be produced only in small amounts or to not be secreted. Possibly, in Campopleginae carrying polydnaviruses, the host-modifying activities of venom became. redundant following the acquisition of polydnaviruses by the lineage.

Published
2013
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23. Phylogenetic character mapping of proteomic diversity shows high correlation with subspecific phylogenetic diversity in Trypanosoma cruzi

Author

Michel Tibayrenc, David Biron, Jenny Telleria, Jean-Paul Brizard, Francisco J. Ayala, Martial Séveno, Edith Demettre, Christian Barnabé, Génétique et évolution des maladies infectieuses (GEMI), Centre National de la Recherche Scientifique (CNRS)-Université Montpellier 1 (UM1)-Institut de Recherche pour le Développement (IRD [France-Sud]), Laboratoire Microorganismes : Génome et Environnement (LMGE), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Centre National de la Recherche Scientifique (CNRS), Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Actualisation et valorisation des données pédologiques tropicales et méditerranéennes. Contributions à la recherche, à l'expertise et à l'aide à la gestion des ressources (VALPEDO), Department of Ecology and Evolutionary Biology, University of California, Université Montpellier 1 (UM1)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and University of California (UC)

Subjects
Proteomics, parallel evolution, Trypanosoma cruzi, infectious disease, 030231 tropical medicine, Protozoan Proteins, Gene Expression, Mass Spectrometry, 03 medical and health sciences, 0302 clinical medicine, Gene mapping, Species Specificity, Phylogenetics, parasitic diseases, Cluster Analysis, Electrophoresis, Gel, Two-Dimensional, Typing, Phylogeny, 030304 developmental biology, 0303 health sciences, disease, Multidisciplinary, Phylogenetic tree, biology, Biodiversity, Biological Sciences, biology.organism_classification, Molecular biology, 3. Good health, Phylogenetic diversity, Genetic distance, Sister group, Evolutionary biology, Chagas, parasite, gene expression, [SDE.BE]Environmental Sciences/Biodiversity and Ecology
Abstract

We performed a phylogenetic character mapping on 26 stocks of Trypanosoma cruzi , the parasite responsible for Chagas disease, and 2 stocks of the sister taxon T. cruzi marinkellei to test for possible associations between T. cruzi –subspecific phylogenetic diversity and levels of protein expression, as examined by proteomic analysis and mass spectrometry. We observed a high level of correlation ( P < 10 −4 ) between genetic distance, as established by multilocus enzyme electrophoresis, and proteomic dissimilarities estimated by proteomic Euclidian distances. Several proteins were found to be specifically associated to T. cruzi phylogenetic subdivisions (discrete typing units). This study explores the previously uncharacterized links between infraspecific phylogenetic diversity and gene expression in a human pathogen. It opens the way to searching for new vaccine and drug targets and for identification of specific biomarkers at the subspecific level of pathogens.

Published
2010
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24. Blood-feeding and immunogenic Aedes aegypti saliva proteins

Author

Franck Remoue, Ladawan Wasinpiyamongkol, Souleymane Doucoure, Patrick Jouin, David Biron, Pornapat Surasombatpattana, Martial Séveno, Frédéric Thomas, Dorothée Missé, Edith Demettre, Jean-Paul Brizard, Sirilaksana Patramool, Natthanej Luplertlop, François Mouchet, Department of Tropical Hygiene, Faculty of Tropical Medicine, Mahidol University, Bangkok, Thailand, Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Épidémiologie et prévention : environnement et efficacité des interventions (EPIPREV), Institut de Génomique Fonctionnelle (IGF), Centre National de la Recherche Scientifique (CNRS)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 1 (UM1)-Université de Montpellier (UM), Actualisation et valorisation des données pédologiques tropicales et méditerranéennes. Contributions à la recherche, à l'expertise et à l'aide à la gestion des ressources (VALPEDO), Laboratoire Microorganismes : Génome et Environnement (LMGE), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physique et Physiologie Intégratives de l'Arbre Fruitier et Forestier (PIAF), Institut National de la Recherche Agronomique (INRA)-Université Blaise Pascal - Clermont-Ferrand 2 (UBP), ANR, CNRS Interdisciplinaire MIE, Trop.Med, Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Université d'Auvergne - Clermont-Ferrand I (UdA)

Subjects
Saliva, Blood meal, GLANDE SALIVAIRE, Biochemistry, Salivary Glands, Dengue fever, Dengue, 0302 clinical medicine, Aedes, Midgut, Electrophoresis, Gel, Two-Dimensional, 0303 health sciences, biology, medicine.diagnostic_test, Salivary gland, APPAREIL DIGESTIF, Animal proteomics, EXPRESSION DES GENES, 3. Good health, medicine.anatomical_structure, Blood, METABOLISME, REPAS DE SANG, Insect Proteins, MOUSTIQUE, VIRUS, Female, DENGUE, TRANSMISSION, 030231 tropical medicine, Aedes aegypti, Immunofluorescence, Microbiology, glands, 03 medical and health sciences, REPAS, PROTEINE, medicine, Animals, PROTEOMIQUE, Salivary Proteins and Peptides, Molecular Biology, 030304 developmental biology, IMMUNITE, Salivary, VECTEUR, fungi, SANG, medicine.disease, biology.organism_classification, Virology, Animal Feed, PHYSIOLOGIE, [SDE.BE]Environmental Sciences/Biodiversity and Ecology
Abstract

International audience; Mosquito-transmitted pathogens pass through the insect's midgut (MG) and salivary gland (SG). What occurs in these organs in response to a blood meal is poorly understood, but identifying the physiological differences between sugar-fed and blood-fed (BF) mosquitoes could shed light on factors important in pathogens transmission. We compared differential protein expression in the MGs and SGs of female Aedes aegypti mosquitoes after a sugar- or blood-based diet. No difference was observed in the MG protein expression levels but certain SG proteins were highly expressed only in BF mosquitoes. In sugar-fed mosquitoes, housekeeping proteins were highly expressed (especially those related to energy metabolism) and actin was up-regulated. The immunofluorescence assay shows that there is no disruption of the SG cytoskeletal after the blood meal. We have generated for the first time the 2-DE profiles of immunogenic Ae. aegypti SG BF-related proteins. These new data could contribute to the understanding of the physiological processes that appear during the blood meal.

Published
2010
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25. Analysis of virion structural components reveals vestiges of the ancestral ichnovirus genome

Author

Fabrice Legeai, Gabor Gyapay, Fasséli Coulibaly, Patrick Wincker, Anne-Nathalie Volkoff, Catherine Béliveau, Jean-Michel Drezen, Sylvie Samain, Max Bergoin, Véronique Jouan, François Cousserans, Serge Urbach, Bertille Provost, Michel Cusson, Edith Demettre, Biologie Intégrative et Virologie des Insectes [Univ. de Montpellier II] (BIVI), Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2), Institut de Génomique Fonctionnelle (IGF), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), BioCampus Montpellier (BCM), Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Structural Virology Group, Monash University [Clayton], Biologie des organismes et des populations appliquées à la protection des plantes (BIO3P), Institut National de la Recherche Agronomique (INRA)-Université de Rennes (UR)-AGROCAMPUS OUEST, Biological systems and models, bioinformatics and sequences (SYMBIOSE), Institut de Recherche en Informatique et Systèmes Aléatoires (IRISA), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Inria Rennes – Bretagne Atlantique, Institut National de Recherche en Informatique et en Automatique (Inria), Laurentian Forestry Centre, Natural Resources Canada (NRCan), Institut de recherche sur la biologie de l'insecte UMR7261 (IRBI), Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS), ANR-05-BLAN-0199,EVPARASITOID,Physiologie, diversité et évolution des interactions hôte-parasitoïde(2005), ANR-09-BLAN-0243,PARATOXOSE(2009), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-AGROCAMPUS OUEST, Université de Tours-Centre National de la Recherche Scientifique (CNRS), ANR-09-BLAN-0243,PARATOXOSE,Parasitoid Toxins : Origin, Specificity, Evolution(2009), Institut de Génomique d'Evry (IG), Institut de Biologie François JACOB (JACOB), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Virologie moléculaire et structurale (VMS), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Inria Rennes – Bretagne Atlantique, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Legeai, Fabrice, Programme non thématique - Appel à projets de recherche - Physiologie, diversité et évolution des interactions hôte-parasitoïde - - EVPARASITOID2005 - ANR-05-BLAN-0199 - BLANC - VALID, Blanc - - PARATOXOSE2009 - ANR-09-BLAN-0243 - Blanc - VALID, AGROCAMPUS OUEST, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Université de Rennes 1 (UR1), and Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National de la Recherche Agronomique (INRA)

Subjects
0106 biological sciences, Genome, Insect, Wasps, génomique fonctionnelle, 01 natural sciences, Genome, Nudivirus, chemistry.chemical_compound, Proviruses, hyposoter didymator, Convergent evolution, lcsh:QH301-705.5, [INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM], Genetics, 0303 health sciences, [SDV.BIBS] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], noctuelle, biology, Virulence, Polydnavirus, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Virology/Virus Evolution and Symbiosis, 3. Good health, Multigene Family, ENDOPARASITOIDE LARVAIRE, Female, polydnavirus, Bracovirus, Research Article, lcsh:Immunologic diseases. Allergy, food.ingredient, Immunology, virus, Genome, Viral, macromolecular substances, 010603 evolutionary biology, Microbiology, Evolution, Molecular, 03 medical and health sciences, Viral Proteins, food, Virology, Animals, [SDV.MP.PAR]Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology, Molecular Biology, Gene, 030304 developmental biology, RELATION HOTE-PARASITE, STRUCTURE DU GENOME, VIRUS SYMBIOTIQUE, Ovary, fungi, Virion, biology.organism_classification, chemistry, lcsh:Biology (General), Polydnaviridae, Parasitology, Ichnovirus, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM], lcsh:RC581-607, DNA
Abstract

Many thousands of endoparasitic wasp species are known to inject polydnavirus (PDV) particles into their caterpillar host during oviposition, causing immune and developmental dysfunctions that benefit the wasp larva. PDVs associated with braconid and ichneumonid wasps, bracoviruses and ichnoviruses respectively, both deliver multiple circular dsDNA molecules to the caterpillar. These molecules contain virulence genes but lack core genes typically involved in particle production. This is not completely unexpected given that no PDV replication takes place in the caterpillar. Particle production is confined to the wasp ovary where viral DNAs are generated from proviral copies maintained within the wasp genome. We recently showed that the genes involved in bracovirus particle production reside within the wasp genome and are related to nudiviruses. In the present work we characterized genes involved in ichnovirus particle production by analyzing the components of purified Hyposoter didymator Ichnovirus particles by LC-MS/MS and studying their organization in the wasp genome. Their products are conserved among ichnovirus-associated wasps and constitute a specific set of proteins in the virosphere. Strikingly, these genes are clustered in specialized regions of the wasp genome which are amplified along with proviral DNA during virus particle replication, but are not packaged in the particles. Clearly our results show that ichnoviruses and bracoviruses particles originated from different viral entities, thus providing an example of convergent evolution where two groups of wasps have independently domesticated viruses to deliver genes into their hosts., Author Summary The polydnaviruses (PDVs) are a unique virus type used by an organism (a parasitic wasp) to manipulate the physiology of another organism (a lepidopteran host) in order to ensure successful parasitism. The evolutionary origin of these unusual viruses, found in ∼17,500 braconid wasps (Bracoviruses) and ∼15,000 ichneumonid wasps (Ichnoviruses), has been a major question for the last decade. We thus undertook an exclusive work aiming at investigating this origin via the characterization of genes encoding structural components for both types of PDVs. The present paper constitutes the first report on the identity and genome organisation of the viral machinery producing Ichnovirus virions. Our results strongly suggest that Ichnoviruses originated from a virus belonging to a group as yet uncharacterized that integrated its genome into that of an ichneumonid wasp ancestor. More importantly, our results demonstrate that the ancestor of Ichnoviruses differs from that of Bracoviruses, which originated from a nudivirus. We have now identified, for the two types of PDVs, the non packaged viral genes and their products involved in producing particles injected into the host during oviposition. Together, these data provide an example of convergent evolution where different groups of wasps have independently domesticated viruses to deliver genes into their hosts.

Published
2010
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26. Identification of total and differentially expressed excreted-secreted proteins from Trypanosoma congolense strains exhibiting different virulence and pathogenicity

Author

Paul Chuchana, Géraldine Bossard, Alain Boulangé, Zakaria Bengaly, Jean-Paul Brizard, Philippe Vincendeau, Philippe Holzmuller, Pascal Grébaut, Edith Demettre, Martial Séveno, Gérard Cuny, Patrick Jouin, Interactions hôtes-vecteurs-parasites-environnement dans les maladies tropicales négligées dues aux trypanosomatides (UMR INTERTRYP), Université de Bordeaux (UB)-Institut de Recherche pour le Développement (IRD)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad), Laboratoire Génome et développement des plantes (LGDP), Université de Perpignan Via Domitia (UPVD)-Centre National de la Recherche Scientifique (CNRS), Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Parasitologie (EA 3677), Université Bordeaux Segalen - Bordeaux 2, Centre International de Recherche-Développement sur l'Elevage en zones humides (CIRDES), CIRDES, Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut de Recherche pour le Développement (IRD)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Université de Bordeaux (UB)

Subjects
Proteomics, Pathogenic factors, Trypanosoma congolense, Protozoan Proteins, MESH: Virulence, [SDV.BID.SPT]Life Sciences [q-bio]/Biodiversity/Systematics, Phylogenetics and taxonomy, L73 - Maladies des animaux, MESH: Animals, African trypanosomiasis, Electrophoresis, Gel, Two-Dimensional, MESH: Protozoan Proteins, ComputingMilieux_MISCELLANEOUS, Secretome, 2. Zero hunger, 0303 health sciences, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], biology, Virulence, MESH: Proteomics, [SDV.BID.EVO]Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE], [SDV.BBM.MN]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular Networks [q-bio.MN], MESH: Trypanosoma congolense, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], 3. Good health, Infectious Diseases, Proteome, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Trypanosoma brucei, Microbiology, [SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics, 03 medical and health sciences, Species Specificity, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], parasitic diseases, medicine, MESH: Species Specificity, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], 030304 developmental biology, [SDV.GEN]Life Sciences [q-bio]/Genetics, 030306 microbiology, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Trypanosoma evansi, MESH: Electrophoresis, Gel, Two-Dimensional, medicine.disease, biology.organism_classification, Trypanosoma vivax, [SDV.BV.AP]Life Sciences [q-bio]/Vegetal Biology/Plant breeding, MESH: Trypanosomiasis, African, Trypanosomiasis, African, Trypanosoma, Parasitology, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM], Trypanosomiasis
Abstract

Animal trypanosomosis is a major constraint to livestock productivity in the tropics and has a significant impact on the life of millions of people globally (mainly in Africa, South America and south-east Asia). In Africa, the disease in livestock is caused mainly by Trypanosoma congolense, Trypanosoma vivax, Trypanosoma evansi and Trypanosoma brucei brucei. The extracellular position of trypanosomes in the bloodstream of their host requires consideration of both the parasite and its naturally excreted-secreted factors (secretome) in the course of pathophysiological processes. We therefore developed and standardised a method to produce purified proteomes and secretomes of African trypanosomes. In this study, two strains of T. congolense exhibiting opposite properties of both virulence and pathogenicity were further investigated through their secretome expression and its involvement in host-parasite interactions. We used a combined proteomic approach (one-dimensional SDS-PAGE and two-dimensional differential in-gel electrophoresis coupled to mass spectrometry) to characterise the whole and differentially expressed protein contents of secretomes. The molecular identification of differentially expressed trypanosome molecules and their correlation with either the virulence process or pathogenicity are discussed with regard to their potential as new diagnostic or therapeutic tools against animal trypanosomosis.

Published
2008
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27. Interplay between MgtC and PagC in Salmonella enterica serovar Typhimurium

Author

Anne-Béatrice Blanc-Potard, Cécile Rang, Eric Alix, Christine Felix, Nara Figueroa-Bossi, Edith Demettre, Tsuyoshi Miki, LPHI - Laboratory of Pathogen Host Interactions (LPHI), and Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Serotype, Salmonella typhimurium, [SDV]Life Sciences [q-bio], Mutant, Microbiology, 03 medical and health sciences, Mice, Bacterial Proteins, Mutant strain, parasitic diseases, Animals, Cation Transport Proteins, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, SLC11A1, 0303 health sciences, Mice, Inbred BALB C, Mice, Inbred C3H, biology, 030306 microbiology, Macrophages, Membrane Proteins, Gene Expression Regulation, Bacterial, Null mutant, biology.organism_classification, Enterobacteriaceae, Infectious Diseases, Salmonella enterica, Mutation, Salmonella Infections, biology.protein, Female, Bacteria
Abstract

In Salmonella enterica serovar Typhimurium, MgtC and PagC are positively regulated by the PhoP–PhoQ two-component system, which is activated under magnesium deprivation. Both MgtC and PagC are of unknown function but have been involved in intramacrophage survival. We have found that the amount of PagC is lowered in a ΔmgtC mutant strain grown in magnesium depleted medium. However, the effect of MgtC on PagC does not account for the growth defect of a ΔmgtC mutant in macrophages since, in contrast to previous reports, our results indicate that PagC does not contribute to intramacrophage survival. In addition, a pagC null mutant is only poorly attenuated in Nramp1-negative or Nramp1-positive mice. On the other hand, a mgtC null mutant is significantly more attenuated with Nramp1-positive than Nramp1-negative mice, suggesting that a functional Nramp1 (Slc11a1) further limits the multiplication of this mutant within the host.

Published
2008
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28. Malaria Plasmodium agent induces alteration in the head proteome of their Anopheles mosquito host

Author

Laure Le Bourligu, Thierry Lefèvre, Alex Schwartz, David Biron, François Renaud, Stéphanie Blandin, Frédéric Thomas, Edith Demettre, Elena A. Levashina, Jean-Paul Brizard, Transmission-Interactions-Adaptations hôtes/vecteurs/pathogènes (MIVEGEC-TRIAD), Evolution des Systèmes Vectoriels (ESV), Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Réponse immunitaire et developpement chez les insectes (RIDI - UPR 9002), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de Recherche pour le Développement (IRD), Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Microorganismes : Génome et Environnement (LMGE), Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg (UNISTRA)-Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Centre National de la Recherche Scientifique (CNRS)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 1 (UM1)-Université de Montpellier (UM)

Subjects
Central Nervous System, Proteomics, Plasmodium berghei, Anopheles gambiae, [SDV]Life Sciences [q-bio], malaria, Down-Regulation, Disease Vectors, Biochemistry, Plasmodium, Mass Spectrometry, Host-Parasite Interactions, Apicomplexa, 03 medical and health sciences, 2 DE, 0302 clinical medicine, parasitic diseases, host parasite systems, Anopheles, Animals, Electrophoresis, Gel, Two-Dimensional, Heat shock, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, mosquitoes, [SDV.EE]Life Sciences [q-bio]/Ecology, environment, 0303 health sciences, biology, MS, biology.organism_classification, Virology, 3. Good health, Cell biology, Malaria, Up-Regulation, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Proteome, Head, 030217 neurology & neurosurgery, [SDV.EE.IEO]Life Sciences [q-bio]/Ecology, environment/Symbiosis
Abstract

Despite increasing evidence of behavioural manipulation of their vectors by pathogens, the underlying mechanisms causing infected vectors to act in ways that benefit pathogen transmission remain enigmatic in most cases. Here, 2-D DIGE coupled with MS were employed to analyse and compare the head proteome of mosquitoes (Anopheles gambiae sensu stricto (Giles)) infected with the malarial parasite (Plasmodium berghei) with that of uninfected mosquitoes. This approach detected altered levels of 12 protein spots in the head of mosquitoes infected with sporozoites. These proteins were subsequently identified using MS and functionally classified as belonging to metabolic, synaptic, molecular chaperone, signalling, and cytoskeletal groups. Our results indicate an altered energy metabolism in the head of sporozoite-infected mosquitoes. Some of the up-/down-regulated proteins identified, such as synapse-associated protein, 14-3-3 protein and calmodulin, have previously been shown to play critical roles in the CNS of both invertebrates and vertebrates. Furthermore, a heat shock response (HSP 20) and a variation of cytoarchitecture (tropomyosins) have been shown. Discovery of these proteins sheds light on potential molecular mechanisms that underlie behavioural modifications and offers new insights into the study of intimate interactions between Plasmodium and its Anopheles vector.

Published
2007
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29. Food vacuole proteome of the malarial parasite Plasmodium falciparum

Author

Mauld M Lamarque, Jean-François Dubremetz, Patrick Jouin, Joël Poncet, Henri Vial, Christophe Tastet, and Edith Demettre

Subjects
biology, medicine.diagnostic_test, Clinical Biochemistry, Plasmodium falciparum, biology.organism_classification, Proteomics, Cell biology, Apicomplexa, Western blot, Organelle, Proteome, medicine, Food vacuole, Biogenesis
Abstract

The Plasmodium falciparum food vacuole (FV) is a lysosome-like organelle where erythrocyte hemoglobin digestion occurs. It is a favorite target in the development of antimalarials. We have used a tandem mass spectrometry approach to investigate the proteome of an FV-enriched fraction and identified 116 proteins. The electron microscopy analysis and the Western blot data showed that the major component of the fraction was the FV and, as expected, the majority of previously known FV markers were recovered. Of particular interest, several proteins involved in vesicle-mediated trafficking were identified, which are likely to play a key role in FV biogenesis and/or FV protein trafficking. Recovery of parasite surface proteins lends support to the cytostomal pathway of hemoglobin ingestion as a FV trafficking route. We have identified 32 proteins described as hypothetical in the databases. This insight into FV protein content provides new clues towards understanding the biological function of this organelle in P. falciparum.

Published
2007

30. RNase L levels in peripheral blood mononuclear cells: 37-kilodalton/83-kilodalton isoform ratio is a potential test for chronic fatigue syndrome

Author

Kiet Tiev, Edith Demettre, L. Bastide, Bernard Lebleu, Philippe Ercolano, and Jean Cabane

Subjects
Microbiology (medical), Gene isoform, Adult, Male, medicine.medical_specialty, RNase P, Clinical Biochemistry, Immunology, Population, Peripheral blood mononuclear cell, Sensitivity and Specificity, Kilodalton, Internal medicine, Endoribonucleases, Chronic fatigue syndrome, Immunology and Allergy, Medicine, Humans, Prospective Studies, Prospective cohort study, education, Letters to the Editor, education.field_of_study, Fatigue Syndrome, Chronic, business.industry, Case-control study, Middle Aged, medicine.disease, Molecular Weight, Endocrinology, Immune-Mediated Responses and Disorders, Case-Control Studies, Leukocytes, Mononuclear, Female, business
Abstract

Chronic fatigue syndrome (CFS) is a disorder characterized by debilitating fatigue associated with immunological abnormalities. The etiology remains unclear. A low-molecular-mass (37 kDa) isoform of RNase L has been described in peripheral blood mononuclear cell (PBMC) extracts, and the ratio of two isoforms of RNase L (37 kDa/83 kDa) has been proposed as a potential biochemical marker of CFS. In a prospective case-control study, we tested whether the RNase L 37-kDa/83-kDa ratio could discriminate a SFC population. We compared the ratio of RNase L isoforms in PBMCs from 11 patients with CFS (6 women and 5 men; mean age ± standard deviation, 43.2 ± 13.8 years) and PBMCs from 14 healthy well-matched volunteers (10 women and 4 men; age, 39.1 ± 11.6 years). A ratio of RNase L of 0.4 used as a threshold allowed diagnosis of CFS with high sensitivity (91%; 95% confidence interval [CI], 57 to 99%) and specificity (71%; 95% CI, 41 to 90%). The positive and negative prognostic values were 71% (95% CI, 41 to 90%) and 91% (95% CI, 57 to 99%), respectively. In the absence of acute infection or chronic inflammation, a high RNase L ratio could distinguish CFS patients from healthy volunteers. Additional large studies and follow-up studies are required to confirm the stability of this high ratio of RNase L isoforms in a CFS group.

Published
2003

31. Ribonuclease L

Author

A. D'haese, Bernard Lebleu, Karen De Smet, C. Vincent Herst, Karim El Bakkouri, Patrick Englebienne, Marc Frémont, Edith Demettre, Lionel Bastide, and Simon Roelens

Subjects
Biochemistry, biology, Chemistry, biology.protein, Ribonuclease L
Published
2002
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33. Ribonuclease L Inhibitor

Author

C. Vincent Herst, Bernard Lebleu, Patrick Englebienne, Edith Demettre, Kenny De Meirleir, A. D'haese, and Lionel Bastide

Subjects
biology, Chemistry, biology.protein, ATP-binding cassette transporter, SUPERFAMILY, Molecular biology, Ribonuclease L
Published
2002
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34. A 37 kDa 2-5A binding protein as a potential biochemical marker for chronic fatigue syndrome

Author

Kenny De Meirleir, Tamim Salehzada, Catherine Bisbal, Isabelle Campine, Edith Demettre, Bernard Lebleu, Pascale De Becker, Human Physiology and General Biochemistry, and Vrije Universiteit Brussel

Subjects
medicine.medical_specialty, Pathology, biology, business.industry, Binding protein, General Medicine, medicine.disease, Control subjects, Peripheral blood mononuclear cell, Endocrinology, Fibromyalgia, Internal medicine, medicine, biology.protein, Chronic fatigue syndrome, Distribution (pharmacology), business, Depression (differential diagnoses), Ribonuclease L
Abstract

PURPOSE: Recent studies have revealed abnormalities in the ribonuclease L pathway in peripheral blood mononuclear cells of patients with the chronic fatigue syndrome. We conducted a blinded study to detect possible differences in the distribution of 2-5A binding proteins in the cells of patients with chronic fatigue syndrome and controls. PATIENTS AND METHODS: We studied 57 patients with chronic fatigue syndrome and 53 control subjects (28 healthy subjects and 25 patients with depression or fibromyalgia). A radioactive probe was used to label 2-5A binding proteins in unfractionated peripheral blood mononuclear cell extracts and to compare their distribution in the three groups. RESULTS: A 37 kDa 2-5A binding polypeptide was found in 50 (88%) of the 57 patients with chronic fatigue syndrome compared with 15 (28%) of the 53 controls ( P 0.05, compared with 3 (11%) of the 28 healthy subjects and none of the patients with fibromyalgia or depression. CONCLUSION: The presence of a 37 kDa 2-5A binding protein in extracts of peripheral blood mononuclear cells may distinguish patients with chronic fatigue syndrome from healthy subjects and those suffering from other diseases.

Published
1999

35. Corrigendum to 'Venom gland extract is not required for successful parasitism in the polydnavirus-associated endoparasitoid Hyposoter didymator (Hym. Ichneumonidae) despite the presence of numerous novel and conserved venom proteins' [Insect Biochem. Mol. Biol. 43 (2013), 292–307]

Author

Tristan Dorémus, Dominique Colinet, Marylène Poirié, Eric Wajnberg, Julie Poulain, Véronique Jouan, Carole Azéma-Dossat, Serge Urbach, Edith Demettre, François Cousserans, Anne-Nathalie Volkoff, Jean-Luc Gatti, Isabelle Darboux, Marc Ravallec, and Jean-Michel Escoubas

Subjects
biology, Polydnavirus, media_common.quotation_subject, Parasitism, Venom, Insect, Venom gland, biology.organism_classification, Biochemistry, Hyposoter didymator, Ichneumonidae, Insect Science, Botany, Mole, Molecular Biology, media_common
Published
2014
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36. Variability of the RNase L Isoform Ratio (37 Kilodaltons/83 Kilodaltons) in Diagnosis of Chronic Fatigue Syndrome

Author

Bernard Lebleu, Kiet Tiev, Jean Cabane, M. Briant, Edith Demettre, and M Ziani

Subjects
Adult, musculoskeletal diseases, Microbiology (medical), Gene isoform, medicine.medical_specialty, Pathology, RNase P, Clinical Biochemistry, Immunology, Peripheral blood mononuclear cell, Isozyme, Internal medicine, Endoribonucleases, Chronic fatigue syndrome, Humans, Immunology and Allergy, Medicine, Letter to the Editor, Fatigue Syndrome, Chronic, business.industry, Case-control study, virus diseases, Middle Aged, medicine.disease, Pathophysiology, Isoenzymes, Molecular Weight, Endocrinology, Case-Control Studies, Leukocytes, Mononuclear, Etiology, business
Abstract

Chronic fatigue syndrome (CFS) is a disorder characterized by debilitating fatigue whose etiology and pathophysiology remain unclear. Previous studies showed abnormalities of the RNase L pathway in peripheral blood mononuclear cells (PBMC) from patients with CFS ([1][1], [2][2]). The ratio of RNase

Published
2005
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