Éditeur(s) : HAL CCSD Elsevier
Résumé : The Authors. Published by Elsevier Masson SAS on behalf of Institut Pasteur. This is an open access article under the CC BY-NC-ND license(http://creativecommons.org/licenses/by-nc-nd/4.0/)
Ehrlichia is a large genus of obligate intracellular Gram-negative bacteria transmitted by ticks that cause several emerging infectious diseases in humans and are pathogenic on rodents, ruminants, and dogs. Ehrlichia spp. invade and replicate either in endothelial cells, white blood cells, or within midgut cells and salivary glands of their vector ticks. In this review, we discuss the insights that functional studies are providing on how this group of bacteria exploits their host by subverting host innate immunity and hijacking cellular processes.
ISSN: 1286-4579

hal-01512099
https://hal.archives-ouvertes.fr/hal-01512099
https://hal.archives-ouvertes.fr/hal-01512099/document
https://hal.archives-ouvertes.fr/hal-01512099/file/Moumene%202016%20Microbes%20and%20Infection_%7BEFBE9395-9C1F-4C96-A09E-A017DC15F940%7D.pdf
DOI : 10.1016/j.micinf.2015.11.001

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