Complexomics study of two Helicobacter pylori strains of two pathological origins: Potential targets for vaccine development and new insight in bacteria metabolism
Molecular & Cellular Proteomics. 2010-12-01; 9(12): 2796-2826
DOI: 10.1074/mcp.M110.001065
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1. Mol Cell Proteomics. 2010 Dec;9(12):2796-826. doi: 10.1074/mcp.M110.001065. Epub
2010 Jul 7.
Complexomics study of two Helicobacter pylori strains of two pathological
origins: potential targets for vaccine development and new insight in bacteria
metabolism.
Bernarde C(1), Lehours P, Lasserre JP, Castroviejo M, Bonneu M, Mégraud F, Ménard
A.
Author information:
(1)INSERM U853, 33076 Bordeaux, France.
Helicobacter pylori infection plays a causal role in the development of gastric
mucosa-associated lymphoid tissue (MALT) lymphoma (LG-MALT) and duodenal ulcer
(DU). Although many virulence factors have been associated with DU, many
questions remain unanswered regarding the evolution of the infection toward this
exceptional event, LG-MALT. The present study describes and compares the
complexome of two H. pylori strains, strain J99 associated with DU and strain B38
associated with LG-MALT, using the two-dimensional blue native/SDS-PAGE method.
It was possible to identify 90 different complexes (49 and 41 in the B38 and J99
strains, respectively); 12 of these complexes were common to both strains (seven
and five in the membrane and cytoplasm, respectively), reflecting the variability
of H. pylori strains. The 44 membrane complexes included numerous outer membrane
proteins, such as the major adhesins BabA and SabA retrieved from a complex in
the B38 strain, and also proteins from the hor family rarely studied. BabA and
BabB adhesins were found to interact independently with HopM/N in the B38 and J99
strains, respectively. The 46 cytosolic complexes essentially comprised proteins
involved in H. pylori physiology. Some orphan proteins were retrieved from
heterooligomeric complexes, and a function could be proposed for a number of them
via the identification of their partners, such as JHP0119, which may be involved
in the flagellar function. Overall, this study gave new insights into the
membrane and cytoplasm structure, and those which could help in the design of
molecules for vaccine and/or antimicrobial agent development are highlighted.
DOI: 10.1074/mcp.M110.001065
PMCID: PMC3101863
PMID: 20610778 [Indexed for MEDLINE]