Listeria monocytogenesSurface Proteins: from Genome Predictions to Function

Abstract

SUMMARY 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.

LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species

“…Adherence of L. monocytogenes to the host cell surface is an important event during infection, and involves a number of cell surface proteins, including internalins, Ami and FbpA (Bierne & Cossart, 2007). We previously reported the significance of LAP as a pathogenic factor in L. monocytogenes, promoting bacterial adhesion to intestinal epithelial cells by interacting with mammalian receptor Hsp60 Pandiripally et al, 1999;Wampler et al, 2004).…”

“…For example, InlA with its LPXTG motif forms a cross-link with the sortase substrate, while InlB with its GW (glycine tryptophan) modules interacts with lipoteichoic acid in the cell wall (Bierne & Cossart, 2007). Metabolic or housekeeping enzymes that serve as adhesion/ invasion factors are often referred to as 'anchorless adhesins' (Pancholi & Chhatwal, 2003;Scott & Barnett, 2006) and the mechanism by which they interact with the cell wall is not well understood.…”

Cytoskeleton rearrangements during Listeria infection: Clathrin and septins as new players in the game

“…Thus, entry of bacteria into cells and their intracytosolic replication represent initiating events for tissue dissemination, and a strategy to replicate in a protected environment, thereby presumably avoiding various antibacterial host defenses L. monocytogenes employs a variety of proteins, and in particular members of a protein family known as the internalins, to adhere to and invade host cells. Internalins are members of the Leucine Rich Repeat (LRR) superfamily, a diverse group of proteins characterized by tandem arrays of LRRs [Bierne and Cossart, 2007]. The two major invasion proteins are internalin (InlA) and InlB.…”

Genome-wide transcriptional profiling of the cell envelope stress response and the role of LisRK and CesRK in Listeria monocytogenes

“…adhesion, invasion of host cells and interaction with the immune system (Bierne & Cossart, 2007). In response to the presence of cefuroxime, lmo2522 was found to be the most highly upregulated gene in L. monocytogenes (34-fold induction, Supplementary Table S2).…”

“…In response to the presence of cefuroxime, lmo2522 was found to be the most highly upregulated gene in L. monocytogenes (34-fold induction, Supplementary Table S2). lmo2522 encodes a putative cell wall-binding protein containing a LysM domain, which is thought to be a general peptidoglycan binding module (Bierne & Cossart, 2007). lmo2714, encoding a LPXTG surface protein, was induced more than sixfold by cefuroxime exposure (Supplementary Table S2).…”