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Your search keyword '"MESH: Helicobacter Infections/microbiology"' showing total 4 results
Start Over Descriptor "MESH: Helicobacter Infections/microbiology" Topic gastric mucosa
4 results on '"MESH: Helicobacter Infections/microbiology"'

1. Helicobacter pylori Adapts to Chronic Infection and Gastric Disease via pH-Responsive BabA-Mediated Adherence

Author

Verena Königer, D. Scott Merrell, Roman Andriiovych Moskalenko, Rainer Haas, Thomas Borén, Sara Henriksson, Jafar Mahdavi, Abhijit Chowdhury, Johan Ögren, Anders Hofer, Jay V. Solnick, Dan Danielsson, Sara K. Lindén, Dag Ilver, Konstantinos S. Papadakos, Susanne Vikström, Jörgen Ådén, Jan Holgersson, Gerhard Gröbner, Alexej Schmidt, Jeanna Bugaytsova, Oscar Björnham, Göran O. Bylund, Rolf Sjöström, Stefan Oscarson, Dionyssios N. Sgouras, Lori M. Hansen, Yevgen A Chernov, Anders Esberg, Kristof Moonens, Christopher Aisenbrey, Charles Kelly, Ludmilla A. Morozova-Roche, Jeannette M. Whitmire, Beatriz Martinez-Gonzalez, Asish K. Mukhopadhyay, Angela Eldridge, Nicklas Strömberg, Robert H. Gilman, Andre Dubois, Lars Engstrand, Staffan Schedin, Brett A. Chromy, Justine Younson, Matthew Goldman, Anna Shevtsova, Macarena P. Quintana-Hayashi, Hui Liu, Magnus Unemo, Lena Rakhimova, Anna Åberg, Sebastian Suerbaum, Anna Arnqvist, Pär Gideonsson, Maréne Landström, Douglas E. Berg, Kristoffer Brännström, Anders Olofsson, Melissa Mendez, G. Balakrish Nair, Han Remaut, Umeå University, School of Life Sciences, University of Nottingham, UK (UON), Sahlgrenska Academy at University of Gothenburg [Göteborg], Université libre de Bruxelles (ULB), VIB-VUB Center for Structural Biology [Bruxelles], VIB [Belgium], Sumy State University, Max Von Pettenkofer Institute (MVP), Ludwig-Maximilians-Universität München (LMU), Uniformed Services University of the Health Sciences (USUHS), King‘s College London, Johns Hopkins Bloomberg School of Public Health [Baltimore], Johns Hopkins University (JHU), School of Digestive and Liver Diseases [Kolkata] (SDLD), National Institute of Cholera and Enteric Diseases, Translational Health Science and Technology Institute [Faridabad] (THSTI), Institut Pasteur Hellénique, Réseau International des Instituts Pasteur (RIIP), Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Karolinska Institutet [Stockholm], Örebro University Hospital [Örebro, Sweden], Hannover Medical School [Hannover] (MHH), German Center for Infection Research - partner site Hannover-Braunschweig (DZIF), School of Chemistry and Chemical Biology (UCD), University College Dublin [Dublin] (UCD), University of California [Davis] (UC Davis), University of California, German Center for Infection Research, Partnersite Munich (DZIF), Département d'Informatique [Bruxelles] (ULB), Faculté des Sciences [Bruxelles] (ULB), Université libre de Bruxelles (ULB)-Université libre de Bruxelles (ULB), University of California [San Diego] (UC San Diego), This work was supported by grants from Vetenskapsrådet (VR/M) to T.B. and S.K.L., Cancerfonden to T.B. and A.A., VR/NT to A.A. and S. Schedin, Formas to S.K.L., the J.C. Kempe and Seth M. Kempe Memorial Foundation, the Knut and Alice Wallenberg Foundation (2012.0090) to T.B. and M.L., European Union Seventh Framework Program GastricGlycoExplorer ITN grant number 316929 to T.B. and Y.A.C., Magn. Bergvall’s Foundation to S. Schedin, DFG (SFB 900/A1) to S. Suerbaum, DFG (HA2697/16-1) to R.H., FP6 ANR-06-PATHO-00701 ERA-NET and Actions Concertées Inter-Pasteuriennes (ACIP) (2006) to D.N.S., NIH R01DK063041 to D.E.B., NIH CA082312 to D.S.M., NIH AI070803 and AI081037 to J.V.S., CSIR project, India (No. 37(1640)/14/EMR –II) to A.K.M., and VIB and FWO (grants: G033717N and 12H8416N) to K.M. and H.R., This paper is dedicated to the memory of our friend, collaborator, and co-author Dr. Andre Dubois, a great scientist who contributed importantly both intellectually and materially to this project. We thank S. Michopoulos and G. Mantzaris for H. pylori clinical isolates and Ö. Furberg (NoPolo.se), N. Ulander (softplanbangkok.com), S. Lindström, and M. Borén for the digital movie, tech, art, and figure work, respectively., Vrije Universiteit Brussel, Basic (bio-) Medical Sciences, Structural Biology Brussels, and Department of Bio-engineering Sciences

Subjects
0301 basic medicine, MESH: Hydrogen-Ion Concentration, Gastric acidity, MESH: Helicobacter Infections/pathology, MESH: Helicobacter pylori/physiology, Disease, adaptation, Bacterial Adhesion, polymorphism, acid responsiveness, MESH: Bacterial Adhesion, Bacterial, Hydrogen-Ion Concentration, gastric acidity, Adhesins, 3. Good health, Cell and molecular biology, medicine.anatomical_structure, Infectious Diseases, MESH: Gastric Mucosa/microbiology, Medical Microbiology, 030106 microbiology, Immunology, Digestive Diseases - (Peptic Ulcer), Biology, blood group antigen-binding adhesion, Microbiology, Helicobacter Infections, diversity, Vaccine Related, 03 medical and health sciences, Virology, ABO blood group system, Biodefense, Gastric mucosa, medicine, MESH: Helicobacter Infections/microbiology, multimerization, Adhesins, Bacterial, subpopulations, Helicobacter pylori, Prevention, gastric cancer, MESH: Adhesins, Bacterial/metabolism, biology.organism_classification, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH: Gastric Mucosa/pathology, Bacterial adhesin, Chronic infection, 030104 developmental biology, Emerging Infectious Diseases, Gastric Mucosa, Parasitology, Digestive Diseases
Abstract

The BabA adhesin mediates high-affinity binding of Helicobacter pylori to the ABO blood group antigen-glycosylated gastric mucosa. Here we show that BabA is acid responsive-binding is reduced at low pH and restored by acid neutralization. Acid responsiveness differs among strains; often correlates with different intragastric regions and evolves during chronic infection and disease progression; and depends on pH sensor sequences in BabA and on pH reversible formation of high-affinity binding BabA multimers. We propose that BabA's extraordinary reversible acid responsiveness enables tight mucosal bacterial adherence while also allowing an effective escape from epithelial cells and mucus that are shed into the acidic bactericidal lumen andthat bio-selection and changes in BabA bindingproperties through mutation and recombination with babA-related genes are selected by differencesamong individuals and by changes in gastric acidity over time. These processes generate diverse H.pylori subpopulations, in which BabA's adaptive evolution contributes to H.pylori persistence and overt gastric disease.

Published
2017

2. Anti-Helicobacter pylori activities of natural isopentenyloxycinnamyl derivatives from Boronia pinnata

Author

Valérie Michel, Marie-Christine Prévost, Cécile Ribeiro da Silva, Francesco Epifano, Eliette Touati, Salvatore Genovese, Pathogenèse de Helicobacter, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Dipartimento di Scienze del Farmaco, Università degli studi 'G. d'Annunzio' Chieti-Pescara [Chieti-Pescara] (Ud'A), Microscopie Ultrastructurale (Plate-forme), This work was funded by the OdysseyRe Company. C. Ribeiro da Silva received a fellowship from the Erasmus program for training students from Escola Superior de Biotecnologia, Catholic University of Porto (Portugal) under the EC’s Leonardo program., and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Male, Plant Science, MESH: Helicobacter pylori/growth & development, Bacterial growth, Mice, MESH: Anti-Bacterial Agents/pharmacology, Drug Discovery, MESH: Animals, MESH: Microbial Sensitivity Tests, 0303 health sciences, biology, Chemistry, MESH: Helicobacter Infections/drug therapy, Stomach, General Medicine, Plant secondary metabolites, Boronia pinnata, 3. Good health, Anti-Bacterial Agents, MESH: Helicobacter pylori/ultrastructure, medicine.anatomical_structure, Oxyprenylated derivatives, MESH: Stomach/microbiology, MESH: Microscopy, Electron, Scanning, Microbial Sensitivity Tests, Helicobacter pylori infection, Mouse model, Microbiology, Helicobacter Infections, MESH: Cinnamates/pharmacology, 03 medical and health sciences, MESH: Mice, Inbred C57BL, In vivo, Gastric mucosa, medicine, MESH: Cinnamates/isolation & purification, Animals, MESH: Mice, Rutaceae, MESH: Helicobacter Infections/microbiology, 030304 developmental biology, Pharmacology, MESH: Rutaceae/chemistry, Helicobacter pylori, MESH: Anti-Bacterial Agents/isolation & purification, 030306 microbiology, biology.organism_classification, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH: Male, In vitro, Mice, Inbred C57BL, Complementary and alternative medicine, Cinnamates, Anti-bacterial compounds, MESH: Helicobacter pylori/drug effects, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Microscopy, Electron, Scanning, Bacterial cellular morphologies
Abstract

International audience; In this study we investigated the anti-Helicobacter pylori activity of four isopentenyloxycinnamyl derivatives from the Australian shrub Boronia pinnata Sm. (Rutaceae), structurally related to boropinic acid: (E)-3-(4-(3-methylbut-2-enyloxy)-3,5-dimethoxyphenyl)acrylaldehyde (1), boropinol C (2), boropinal (3) and boropinol A (4). In vitro growth of H. pylori strains 26695 and B128 was analyzed in liquid culture with increasing doses of these compounds. Bacterial morphology was visualized by scanning electron microscopy. The in vivo effects of the two most efficient molecules that reduced bacterial growth in vitro, compounds 3 and 4, were investigated on H. pylori gastric colonization in the mouse model. The presence of these compounds in the bacterial cultures led to alterations of bacterial surface and flagella. In vivo, both compounds 3 and 4 at 250 microM reduced significantly the ability of H pylori to colonize the gastric mucosa of mice, compared with untreated ones. These data indicate that these natural isopentenyloxycinnamyl derivatives related to boropinic acid can be considered as novel antibacterial agents with anti-H. pylori activity.

Published
2012

3. Docosahexaenoic Acid Inhibits Helicobacter pylori Growth In Vitro and Mice Gastric Mucosa Colonization

Author

José Carlos Machado, Rui M. Ferreira, Marta Correia, Valérie Michel, Maria José Oliveira, Patricia Almeida Carvalho, Eliette Touati, Raquel Seruca, Michel Huerre, Ceu Figueiredo, Marie-Agnès Dillies, A. Alves de Matos, Pathogenèse de Helicobacter, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Hospital Curry Cabral [Lisbon, Portugal], Universidade do Porto, Transcriptome et Epigénome (PF2), Institut Pasteur [Paris], Histotechnologie et Pathologie, The Fundação para a Ciência e a Tecnologia (FCT), Portugal, provided funds for this study and to Dr. Correia by a PhD fellowship BD/36689/2007. The Acções integradas Luso-Francesas (CRUP-PAULIF) Portugal and France also provided financial support (AF-8/09)., Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Universidade do Porto = University of Porto, and Institut Pasteur [Paris] (IP)

Subjects
Male, MESH: Helicobacter Infections/pathology, MESH: Helicobacter pylori/drug effects, lcsh:Medicine, MESH: Anti-Bacterial Agents/pharmacology, MESH: Gastric Mucosa/microbiology, Biochemistry, Mice, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Gastrointestinal Infections, MESH: Animals, Bacterial Physiology, lcsh:Science, 0303 health sciences, Multidisciplinary, biology, MESH: Helicobacter Infections/drug therapy, Fatty Acids, food and beverages, Lipids, 3. Good health, Anti-Bacterial Agents, Bacterial Biochemistry, Bacterial Pathogens, medicine.anatomical_structure, Infectious Diseases, MESH: Helicobacter pylori/ultrastructure, MESH: Anti-Bacterial Agents/administration & dosage, Docosahexaenoic acid, MESH: Gastritis/pathology, Gastritis, Medicine, lipids (amino acids, peptides, and proteins), medicine.symptom, Research Article, MESH: Gastritis/drug therapy, Drugs and Devices, Docosahexaenoic Acids, Infectious Disease Control, Inflammation, Gastroenterology and Hepatology, Microbiology, Helicobacter Infections, 03 medical and health sciences, In vivo, MESH: Mice, Inbred C57BL, Gastric mucosa, medicine, MESH: Gastritis/microbiology, Animals, Biology, MESH: Mice, MESH: Helicobacter Infections/microbiology, 030304 developmental biology, Helicobacter pylori, 030306 microbiology, lcsh:R, Bacteriology, biology.organism_classification, bacterial infections and mycoses, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, In vitro, MESH: Male, MESH: Gastric Mucosa/pathology, Mice, Inbred C57BL, MESH: Docosahexaenoic Acids/administration & dosage, Gastric Mucosa, lcsh:Q, Bacteria
Abstract

International audience; H. pylori drug-resistant strains and non-compliance to therapy are the major causes of H. pylori eradication failure. For some bacterial species it has been demonstrated that fatty acids have a growth inhibitory effect. Our main aim was to assess the ability of docosahexaenoic acid (DHA) to inhibit H. pylori growth both in vitro and in a mouse model. The effectiveness of standard therapy (ST) in combination with DHA on H. pylori eradication and recurrence prevention success was also investigated. The effects of DHA on H. pylori growth were analyzed in an in vitro dose-response study and n in vivo model. We analized the ability of H. pylori to colonize mice gastric mucosa following DHA, ST or a combination of both treatments. Our data demonstrate that DHA decreases H. pylori growth in vitro in a dose-dependent manner. Furthermore, DHA inhibits H. pylori gastric colonization in vivo as well as decreases mouse gastric mucosa inflammation. Addition of DHA to ST was also associated with lower H. pylori infection recurrence in the mouse model. In conclusion, DHA is an inhibitor of H. pylori growth and its ability to colonize mouse stomach. DHA treatment is also associated with a lower recurrence of H. pylori infection in combination with ST. These observations pave the way to consider DHA as an adjunct agent in H. pylori eradication treatment.

Published
2012

4. Glycophenotypic alterations induced by Pteridium aquilinum in mice gastric mucosa: synergistic effect with Helicobacter pylori infection

Author

Steven R. Head, Ana Magalhães, Suzanne Papp, Joana Gomes, Valérie Michel, Celso A. Reis, Ana Sofia Carvalho, Gilberto E. Hernandez, Fátima Gärtner, Eliette Touati, Leonor David, Institute of Molecular Pathology and Immunology of the University of Porto (IPATIMUP), Universidade do Porto, The SCRIPPS Research Institute (SCRIPPS), University of California [Los Angeles] (UCLA), University of California-University of California, Pathogenèse de Helicobacter, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), This work was supported by Fundação para a Ciência e a Tecnologia – [FCT (PIC/IC/82716/2007), grant number SFRH/BD/40563/2007 to J.G and SFRH/BPD/75871/2011 to A.M.], and the Programa de Acções Universitárias Integradas Luso-Francesas - PAULIF [grant number LC/HS/ED/2010-308, F-TC04/11]. The resources and collaborative efforts provided by the Consortium for Functional Glycomics were funded by grant NIGMS-GM62116., Universidade do Porto = University of Porto, The Scripps Research Institute [La Jolla, San Diego], and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Bacterial Diseases, Mouse, MESH: Carbohydrate Metabolism, MESH: Helicobacter Infections/pathology, Glycobiology, Biochemistry, Transcriptome, Mice, 0302 clinical medicine, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, MESH: Gastric Mucosa/drug effects, MESH: Animals, Histochemistry, MESH: Helicobacter Infections/complications, 0303 health sciences, Cocarcinogenesis, Multidisciplinary, biology, Enzyme Classes, Immunochemistry, Cancer Risk Factors, Environmental Causes of Cancer, Animal Models, Immunohistochemistry, MESH: Helicobacter pylori/isolation & purification, Enzymes, 3. Good health, Infectious Diseases, Phenotype, medicine.anatomical_structure, Oncology, 030220 oncology & carcinogenesis, Cytochemistry, Carbohydrate Metabolism, Medicine, medicine.symptom, Immunocytochemistry, C1GALT1, Research Article, MESH: Plant Extracts/toxicity, MESH: Pteridium/chemistry, Science, Carbohydrates, Inflammation, [SDV.CAN]Life Sciences [q-bio]/Cancer, MESH: Stomach Neoplasms/complications, MESH: Phenotype, Helicobacter Infections, Microbiology, 03 medical and health sciences, Model Organisms, Stomach Neoplasms, MESH: Cocarcinogenesis, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Glycosyltransferase, Gastric mucosa, medicine, Animals, Biology, MESH: Mice, Carcinogen, MESH: Helicobacter Infections/microbiology, Glycoproteins, Pteridium, 030304 developmental biology, Helicobacter pylori, Plant Extracts, Glycosyltransferases, MESH: Immunohistochemistry, biology.organism_classification, Gastric Mucosa, biology.protein, Pteridium aquilinum, MESH: Stomach Neoplasms/etiology
Abstract

International audience; The bracken fern Pteridium aquilinum is a plant known to be carcinogenic to animals. Epidemiological studies have shown an association between bracken fern exposure and gastric cancer development in humans. The biological effects of exposure to this plant within the gastric carcinogenesis process are not fully understood. In the present work, effects in the gastric mucosa of mice treated with Pteridium aquilinum were evaluated, as well as molecular mechanisms underlying the synergistic role with Helicobacter pylori infection. Our results showed that exposure to Pteridium aquilinum induces histomorphological modifications including increased expression of acidic glycoconjugates in the gastric mucosa. The transcriptome analysis of gastric mucosa showed that upon exposure to Pteridium aquilinum several glycosyltransferase genes were differently expressed, including Galntl4, C1galt1 and St3gal2, that are mainly involved in the biosynthesis of simple mucin-type carbohydrate antigens. Concomitant treatment with Pteridium aquilinum and infection with Helicobacter pylori also resulted in differently expressed glycosyltransferase genes underlying the biosynthesis of terminal sialylated Lewis antigens, including Sialyl-Lewis x. These results disclose the molecular basis for the altered pattern of glycan structures observed in the mice gastric mucosa. The gene transcription alterations and the induced glycophenotypic changes observed in the gastric mucosa contribute for the understanding of the molecular mechanisms underlying the role of Pteridium aquilinum in the gastric carcinogenesis process.

Published
2012

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