Manioc : Portail | resultats 1 - 20 pour la recherche: Ventosa, Miguel

Histoire militaire de la révolution de Saint-Domingue
Auteur(s) : Poyen-Bellisle, Henry de (1839-....)
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Rapport sur les troubles de Saint-Domingue fait au nom de la Commission des colonies, des Comités de salut public, de législation et de marine, réunis. Tome quatrième
Auteur(s) : Garran, Jean-Philippe (1748-1816)
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Statistique générale et particulière de la France et de ses colonies avec une nouvelle description topographique, physique, agricole, politique, industrielle et commerciale T.7
Auteur(s) : Herbin de Halle, Pierre Etienne (1772-18..) Peuchet, Jacques (1758-1830)
Auteurs secondaires : Poirson, Jean-Baptiste (1760-1831) Tardieu, Jean Baptiste Pierre (1746-1816)
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Leyendas puertorriquenas. Tomo segundo
Auteur(s) : Coll y Toste, Cayetano (1850-1930)
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Rapport fait par Eschasseriaux aîné, au nom de la Commission des colonies, sur la division constitutionnelle du territoire français dans les deux Indes : séance du 29 ventôse an V
Auteur(s) : Eschassériaux, Joseph (1753-1823) France. Conseil des Cinq-Cents
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Proteomic Profiling of the Outer Membrane Fraction of the Obligate Intracellular Bacterial Pathogen Ehrlichia ruminantium
Auteur(s) : Moumène, Amal Marcelino, Isabelle Ventosa, Miguel Gros, Olivier Lefrancois, Thierry Vachieri, Nathalie Meyer, Damien Cohelo, Anna V.
Auteurs secondaires : Centre de Coopération Internationale en Recherche Agronomique pour le Développement Instituto de Tecnologia Química e Biológica António Xavier (ITQB) ; Universidade Nova de Lisboa (UNINOVA) Systématique, adaptation, évolution (SAE) ; Université Pierre et Marie Curie - Paris 6 (UPMC) - Centre National de la Recherche Scientifique (CNRS)

Éditeur(s) : HAL CCSD Public Library of Science
Résumé : International audience
The outer membrane proteins (OMPs) of Gram-negative bacteria play a crucial role in virulence and pathogenesis. Identification of these proteins represents an important goal for bacterial proteomics, because it aids in vaccine development. Here, we have developed such an approach for Ehrlichia ruminantium, the obligate intracellular bacterium that causes heartwater. A preliminary whole proteome analysis of elementary bodies, the extracellular infectious form of the bacterium, had been performed previously, but information is limited about OMPs in this organism and about their role in the protective immune response. Identification of OMPs is also essential for understanding Ehrlichia’s OM architecture, and how the bacterium interacts with the host cell environment. First, we developed an OMP extraction method using the ionic detergent sarkosyl, which enriched the OM fraction. Second, proteins were separated via one-dimensional electrophoresis, and digested peptides were analyzed via nano-liquid chromatographic separation coupled with mass spectrometry (LCMALDI-TOF/TOF). Of 46 unique proteins identified in the OM fraction, 18 (39%) were OMPs, including 8 proteins involved in cell structure and biogenesis, 4 in transport/virulence, 1 porin, and 5 proteins of unknown function. These experimental data were compared to the predicted subcellular localization of the entire E. ruminantium proteome, using three different algorithms. This work represents the most complete proteome characterization of the OM fraction in Ehrlichia spp. The study indicates that suitable subcellular fractionation experiments combined with straightforward computational analysis approaches are powerful for determining the predominant subcellular localization of the experimentally observed proteins.We identified proteins potentially involved in E. ruminantium athogenesis, which are good novel targets for candidate vaccines. Thus, combining bioinformatics and proteomics, we discovered new OMPs for E. ruminantium that are valuable data for those investigating new vaccines against this organism. In summary, we provide both pioneering data and novel insights into the pathogenesis of this obligate intracellular bacterium.
ISSN: 1932-6203

hal-01203402
https://hal.univ-antilles.fr/hal-01203402
https://hal.univ-antilles.fr/hal-01203402/document
https://hal.univ-antilles.fr/hal-01203402/file/2015_Moumene_PLOSONE-1.pdf
DOI : 10.1371/journal.pone.0116758

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