The Streptococcal Blr and Slr Proteins Define a Family of Surface Proteins with Leucine-Rich Repeats: Camouflaging by Other Surface Structures

Waldemarsson, Johan; Areschoug, Thomas; Lindahl, Gunnar; Johnsson, Eskil

doi:10.1128/jb.188.2.378-388.2006

Cited by 28 publications

(50 citation statements)

References 63 publications

(69 reference statements)

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“…When expressed in E. faecalis, Streptococcus mutans antigen P1 (SpaP) was identified as molecule located in the cell wall fraction by immunoblotting, whereas it was barely detected by immunofluorescence (19). Recent studies showed that streptococcal capsule or major surface proteins were involved in the camouflage of several surface proteins and could reduce either antibody recognition (for Blr of S. agalactiae and Slr of S. pyogenes [56]) or cell adhesion capacity (for cell wall-anchored proteins in S. pneumoniae [17,37]). Our results with E. faecalis may similarly indicate that cell wall polysaccharides, which include lipoteichoic acid, teichoic acid, a rhamnopolysaccharide, and a variable capsular polysaccharide (18), might hinder detection of and/or access to surface-exposed proteins.…”

Section: Discussionmentioning

confidence: 99%

C-Terminal WxL Domain Mediates Cell Wall Binding in Enterococcus faecalis and Other Gram-Positive Bacteria

Brinster¹,

Furlan²,

Serror³

2007

J Bacteriol

111

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Analysis of the genome sequence of Enterococcus faecalis clinical isolate V583 revealed novel genes encoding surface proteins. Twenty-seven of these proteins, annotated as having unknown functions, possess a putative N-terminal signal peptide and a conserved C-terminal region characterized by a novel conserved domain designated WxL. Proteins having similar characteristics were also detected in other low-G؉C-content grampositive bacteria. We hypothesized that the WxL region might be a determinant of bacterial cell location. This hypothesis was tested by generating protein fusions between the C-terminal regions of two WxL proteins in E. faecalis and a nuclease reporter protein. We demonstrated that the C-terminal regions of both proteins conferred a cell surface localization to the reporter fusions in E. faecalis. This localization was eliminated by introducing specific deletions into the domains. Interestingly, exogenously added protein fusions displayed binding to whole cells of various gram-positive bacteria. We also showed that the peptidoglycan was a binding ligand for WxL domain attachment to the cell surface and that neither proteins nor carbohydrates were necessary for binding. Based on our findings, we propose that the WxL region is a novel cell wall binding domain in E. faecalis and other gram-positive bacteria.Gram-positive bacteria contain a variety of extracellular proteins, some of which are crucial for adaptation and survival in the environment. These proteins participate in various important functions, such as nutrient catabolism, adhesion for niche colonization, translocation, and defense against the host immune system in the case of invading pathogens (35). At this point, cell surface-exposed proteins secreted via the Sec pathway can be classified into the following seven categories according to their means of associating with the cell surface (1, 4, 6, 8): (i) membrane-spanning proteins; (ii) lipoproteins (52, 55); (iii) cell wall-anchored proteins, which are covalently linked to the peptidoglycan at the carboxyl terminus via the LPXTG motif (34, 48); (iv) proteins containing LysM domains that bind to peptidoglycan, most of which are cell wall hydrolases (23, 44, 51); (v) GW proteins, which interact with lipoteichoic acids on the bacterial cell surface and also with mammalian cells (as shown for InlB and Ami of Listeria monocytogenes [2,21,22,33]); (vi) choline-binding proteins, which bind to phosphorylcholine in the cell wall (12); and (vii) proteins containing surface layer homology domains, which interact with peptidoglycan or cell wall-associated polymers, forming a crystalline surface layer (41). The latter class is restricted to bacilli and lactobacilli so far (32). A new C-terminal domain designated WxL was recently predicted based on in silico global genome analyses of Lactobacillus plantarum (25), Lactobacillus coryniformis (47), and Lactobacillus sakei (5). In these studies, neither biological properties nor cell localization was examined.With the ever-increasing availability of bacter...

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Section: Discussionmentioning

confidence: 99%

C-Terminal WxL Domain Mediates Cell Wall Binding in Enterococcus faecalis and Other Gram-Positive Bacteria

Brinster¹,

Furlan²,

Serror³

2007

J Bacteriol

111

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“…This hypothesis is supported by the demonstration that GW repeats bind to cellular proteoglycans and that these interactions are required for efficient entry (87). Other internalin-like proteins, such as E. faecalis EF2686 (ElrA), S. pyogenes Slr, and S. agalactiae BrlD are also buried in the cell wall (28,190). The accessibility of these proteins at the bacterial surface …”

Section: Localizationmentioning

confidence: 95%

Listeria monocytogenesSurface Proteins: from Genome Predictions to Function

Bierne

Cossart

2007

Microbiol Mol Biol Rev

204

257

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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.

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“…The C-terminal portion of YopM was not resolved in the crystal structure and has no significant homology to other proteins. In contrast to YopM, all the other known bacterial LRR proteins contain larger carboxy-terminal domains (6,7,35,44,46,49,62). For example, the IpaH family members of Shigella and the Salmonella effectors SspH1, SspH2, and SlrP are E3 ubiquitin ligases (6,44,49,50,66).…”

Section: Histopathological and Flow Cytometric Analyses Of Spleens Shmentioning

confidence: 99%

The C-Terminal Tail of Yersinia pseudotuberculosis YopM Is Critical for Interacting with RSK1 and for Virulence

et al. 2010

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Yersinia spp. undermine the immune responses of infected animals by translocating Yops directly into host cells with a type III secretion system. YopM, a leucine-rich repeat protein, is a critical virulence factor in infection. YopM localizes to both the nucleus and the cytoplasm in cultured cells, interacts with mammalian p90 ribosomal S6 kinase 1 (RSK1), and causes a decrease in NK cell populations in spleens. Little is known about the molecular interaction between YopM and RSK1 and its significance in pathogenesis. We performed a systematic deletion analysis of YopM in Yersinia pseudotuberculosis to determine which regions are required for RSK1 interactions, nuclear localization, virulence, and changes in immune cell populations during infection of mice. Full-length YopM associated with RSK1 in at least two protein complexes in infected cells, and deletion of its C-terminal tail abrogated all RSK1 interactions. The C-terminal tail was required for tissue colonization, as yopM mutants that failed to interact with RSK1 were as defective for tissue colonization as was a ⌬yopM mutant; however, nuclear localization of YopM was not dependent on its RSK1 interaction. Mutants expressing YopM proteins which do not interact with RSK1 caused more pathology than did the ⌬yopM mutant, suggesting that there are other RSK1-independent functions of YopM. Histopathological and flow cytometric analyses of spleens showed that infection with wild-type Y. pseudotuberculosis caused an influx of neutrophils, while mice infected with yopM mutants had increased numbers of macrophages. Decreases in NK cells after Y. pseudotuberculosis infection did not correlate with YopM expression. In conclusion, the C terminus of YopM is essential for RSK1 interactions and for virulence.

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The Streptococcal Blr and Slr Proteins Define a Family of Surface Proteins with Leucine-Rich Repeats: Camouflaging by Other Surface Structures

Cited by 28 publications

References 63 publications

C-Terminal WxL Domain Mediates Cell Wall Binding in Enterococcus faecalis and Other Gram-Positive Bacteria

C-Terminal WxL Domain Mediates Cell Wall Binding in Enterococcus faecalis and Other Gram-Positive Bacteria

Listeria monocytogenesSurface Proteins: from Genome Predictions to Function

The C-Terminal Tail of Yersinia pseudotuberculosis YopM Is Critical for Interacting with RSK1 and for Virulence

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