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3. Naive Pluripotent and Trophoblastic Stem Cell Lines as a Model for Detecting Missing Proteins in the Context of the Chromosome-Centric Human Proteome Project

Author

Girard, Océane, primary, Lavigne, Régis, additional, Chevolleau, Simon, additional, Onfray, Constance, additional, Com, Emmanuelle, additional, Schmit, Pierre-Olivier, additional, Chapelle, Manuel, additional, Fréour, Thomas, additional, Lane, Lydie, additional, David, Laurent, additional, and Pineau, Charles, additional

Published
2022
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6. Secretome analysis of Trypanosoma cruzi by proteomics studies

Author

Brossas, Jean-Yves, Gulin, Julián Ernesto Nicolás, Bisio, Margarita Maria Catalina, Chapelle, Manuel, Marinach-Patrice, Carine, Bordessoules, Mallaury, Palazon Ruiz, George, Vion, Jeremy, Paris, Luc, Altcheh, Jaime, and Mazier, Dominique

Subjects
Proteomics, Life Cycles, Serum Proteins, Cell Lines, Protozoan Proteins, lcsh:Medicine, Ciencias de la Salud, Protozoology, Biochemistry, Heat Shock Response, Tandem Mass Spectrometry, Chlorocebus aethiops, Medicine and Health Sciences, Parasitología, purl.org/becyt/ford/3.4 [https], lcsh:Science, Cellular Stress Responses, Protozoans, Trypanosoma Cruzi, Eukaryota, purl.org/becyt/ford/3.1 [https], Bioquímica y Biología Molecular, Medicina Básica, Cell Processes, Protozoan Life Cycles, Electrophoresis, Polyacrylamide Gel, purl.org/becyt/ford/3 [https], Biological Cultures, Research Article, Neglected Tropical Diseases, Trypanosoma, CIENCIAS MÉDICAS Y DE LA SALUD, Trypanosoma cruzi, Tecnologías que involucran la identificación de ADN, proteínas y enzimas, y cómo influyen en el conjunto de enfermedades y mantenimiento del bienestar, Research and Analysis Methods, Microbiology, Biotecnología de la Salud, purl.org/becyt/ford/3.3 [https], Virology, parasitic diseases, Parasitic Diseases, Animals, Chagas Disease, Vero Cells, Protozoan Infections, lcsh:R, Host Cells, Organisms, Biology and Life Sciences, Proteins, Cell Biology, Trypomastigotes, Tropical Diseases, Parasitic Protozoans, lcsh:Q, Parasitic Disease, Viral Transmission and Infection, Developmental Biology, Chromatography, Liquid
Abstract

Background: Chagas disease is a debilitating often fatal disease resulting from infection by the protozoan parasite Trypanosoma cruzi. Chagas disease is endemic in 21 countries of the Americas, and it is an emerging disease in other countries as a result of migration. Given the chronic nature of the infection where intracellular parasites persist for years, the diagnosis of T. cruzi by direct detection is difficult, whereas serologic tests though sensitive may yield false-positive results. The development of new rapid test based on the identification of soluble parasitic antigens in serum would be a real innovation in the diagnosis of Chagas disease. Methods: To identify new soluble biomarkers that may improve diagnostic tests, we investigated the proteins secreted by T. cruzi using mass spectrometric analyses of conditioned culture media devoid of serum collected during the emergence of trypomastigotes from infected Vero cells. In addition, we compared the secretomes of two T. cruzi strains from DTU Tc VI (VD and CL Brener). Results: Analysis of the secretome collected during the emergence of trypomastigotes from Vero cells led to the identification of 591 T. cruzi proteins. Three hundred sixty three proteins are common to both strains and most belong to different multigenic super families (i.e. TcS, GP63, MASP, and DGF1). Ultimately we have established a list of 94 secreted proteins, common to both DTU Tc VI strains that do not belong to members of multigene families. Conclusions: This study provides the first comparative analysis of the secretomes from two distinct T. cruzi strains of DTU TcVI. This led us to identify a subset of common secreted proteins that could potentially serve as serum markers for T. cruzi infection. Their potential could now be evaluated, with specific antibodies using sera collected from patients and residents from endemic regions. Fil: Brossas, Jean Yves. Inserm; Francia. Universite de Paris VI; Francia. Hôpital Pitié-Salpêtrière; Francia Fil: Gulin, Julián Ernesto Nicolás. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina. Gobierno de la Ciudad de Buenos Aires. Instituto Multidisciplinario de Investigaciones en Patologías Pediátricas. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto Multidisciplinario de Investigaciones en Patologías Pediátricas.; Argentina Fil: Bisio, Margarita María Catalina. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina. Gobierno de la Ciudad de Buenos Aires. Instituto Multidisciplinario de Investigaciones en Patologías Pediátricas. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto Multidisciplinario de Investigaciones en Patologías Pediátricas.; Argentina Fil: Chapelle, Manuel. Bruker Daltonics; Francia Fil: Marinach Patrice, Carine. Inserm; Francia. Universite de Paris VI; Francia Fil: Bordessoulles, Mallaury. Universite de Paris VI; Francia. Inserm; Francia Fil: Palazon Ruiz, George. Inserm; Francia Fil: Vion, Jeremy. Inserm; Francia Fil: Paris, Luc. Hôpital Pitié-Salpêtrière; Francia. Universite de Paris VI; Francia Fil: Altcheh, Jaime Marcelo. Gobierno de la Ciudad de Buenos Aires. Hospital General de Niños "Ricardo Gutiérrez"; Argentina. Gobierno de la Ciudad de Buenos Aires. Instituto Multidisciplinario de Investigaciones en Patologías Pediátricas. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto Multidisciplinario de Investigaciones en Patologías Pediátricas.; Argentina Fil: Mazier, Dominique. Inserm; Francia. Universite de Paris VI; Francia. Hôpital Pitié-Salpêtrière; Francia

Published
2017

7. In situ isobaric lipid mapping by MALDI–ion mobility separation–mass spectrometry imaging.

Author

Tingting Fu, Janina Oetjen, Chapelle, Manuel, Verdu, Alexandre, Szesny, Matthias, Chaumot, Arnaud, Degli-Esposti, Davide, Geffard, Olivier, Clément, Yohann, Salvador, Arnaud, and Ayciriex, Sophie

Subjects
ION mobility, ION mobility spectroscopy, SPECTROMETRY, LIPID analysis, MASS spectrometry, LIPIDS, ION traps
Abstract

The highly diverse chemical structures of lipids make their analysis directly from biological tissue sections extremely challenging. Here, we report the in situ mapping and identification of lipids in a freshwater crustacean Gammarus fossarum using matrixassisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) in combination with an additional separation dimension using ion mobility spectrometry (IMS). The high-resolution trapped ion mobility spectrometry (TIMS) allowed efficient separation of isobaric/isomeric lipids showing distinct spatial distributions. The structures of the lipids were further characterized by MS/MS analysis. It is demonstrated that MALDI MSI with mobility separation is a powerful tool for distinguishing and localizing isobaric/isomeric lipids. [ABSTRACT FROM AUTHOR]

Published
2020
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8. Secretome analysis of Trypanosoma cruzi by proteomics studies

Author

Brossas, Jean-Yves, primary, Gulin, Julián Ernesto Nicolás, additional, Bisio, Margarita Maria Catalina, additional, Chapelle, Manuel, additional, Marinach-Patrice, Carine, additional, Bordessoules, Mallaury, additional, Palazon Ruiz, George, additional, Vion, Jeremy, additional, Paris, Luc, additional, Altcheh, Jaime, additional, and Mazier, Dominique, additional

Published
2017
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