Listeria monocytogenesSurface Proteins: from Genome Predictions to Function
- 1 June 2007
- journal article
- review article
- Published by American Society for Microbiology in Microbiology and Molecular Biology Reviews
- Vol. 71 (2) , 377-397
- https://doi.org/10.1128/mmbr.00039-06
Abstract
The genome of the human food-borne pathogen Listeria monocytogenes is predicted to encode a high number of surface proteins. This abundance likely reflects the ability of this bacterium to survive in diverse environments, including soil, food, and the human host. This review focuses on the various mechanisms by which listerial proteins are attached at the bacterial surface and their many functions, including peptidoglycan metabolism, protein processing, adhesion to host cells, and invasion of host tissues. Extensive in silico analysis of the domains or motifs present in these mosaic proteins reveals that diverse structural features allow the surface proteome to interact with diverse bacterial or host components. This diversity offers new clues about the molecular bases of Listeria pathogenesis.This publication has 218 references indexed in Scilit:
- Database resources of the National Center for Biotechnology InformationNucleic Acids Research, 2007
- C-Terminal WxL Domain Mediates Cell Wall Binding in Enterococcus faecalis and Other Gram-Positive BacteriaJournal of Bacteriology, 2007
- A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune systemProceedings of the National Academy of Sciences, 2007
- Inactivation of Lgt Allows Systematic Characterization of Lipoproteins fromListeria monocytogenesJournal of Bacteriology, 2007
- Functional Analysis of AtlA, the MajorN-Acetylglucosaminidase ofEnterococcus faecalisJournal of Bacteriology, 2006
- Contribution of Penicillin-Binding Protein Homologs to Antibiotic Resistance, Cell Morphology, and Virulence of Listeria monocytogenes EGDeAntimicrobial Agents and Chemotherapy, 2006
- The cell wall subproteome of Listeria monocytogenesProteomics, 2004
- The Pfam protein families databaseNucleic Acids Research, 2004
- The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD) 1 1Edited by P. E. WightJournal of Molecular Biology, 2000
- HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin‐like foldProtein Science, 2000