Proteomic and Transcriptomic Profiling of Staphylococcus aureus Surface LPXTG-proteins: Correlation with agr Genotypes and Adherence Phenotypes

Ythier, Mathilde; Resch, Grégory; Waridel, Patrice; Panchaud, Alexandre; Gfeller, Aurélie; Majcherczyk, Paul; Quadroni, Manfredo; Moreillon, Philippe

doi:10.1074/mcp.m111.014191

Cited by 38 publications

(32 citation statements)

References 63 publications

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“…It is possible that these molecules are expressed at different stages during infection. In vitro , FnBPs, ClfB and SasG are displayed during early exponential phase regardless of the growth medium (Novick and Jiang, ; Ythier et al ., ), while SdrC expression is more robust during late exponential to stationary phase in RPMI or glucose‐containing TSB (Ythier et al ., ; and our data). Thus, temporal regulation of CWA protein expression may be beneficial for bacteria depending on the environmental conditions (e.g.…”

Section: Discussionmentioning

confidence: 99%

SdrC induces staphylococcal biofilm formation through a homophilic interaction

Barbu

MacKenzie

Foster

et al. 2014

Molecular Microbiology

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Summary The molecular pathogenesis of many Staphylococcus aureus infections involves growth of bacteria as biofilm. In addition to polysaccharide intercellular adhesin (PIA) and extracellular DNA, surface proteins appear to mediate the transition of bacteria from planktonic growth to sessile lifestyle as well as biofilm growth, and can enable these processes even in the absence of PIA expression. However, the molecular mechanisms by which surface proteins contribute to biofilm formation are incompletely understood. Here we demonstrate that self-association of the serine-aspartate repeat protein SdrC promotes both bacterial adherence to surfaces and biofilm formation. However, this homophilic interaction is not required for the attachment of bacteria to abiotic surfaces. We identified the subdomain that mediates SdrC dimerization and subsequent cell-cell interactions. In addition, we determined that two adjacently located amino acid sequences within this subdomain are required for the SdrC homophilic interaction. Comparative amino acid sequence analysis indicated that these binding sites are conserved. In summary, our study identifies SdrC as a novel molecular determinant in staphylococcal biofilm formation and describes the mechanism responsible for intercellular interactions. Furthermore, these findings contribute to a growing body of evidence suggesting that homophilic interactions between surface proteins present on neighboring bacteria induce biofilm growth.

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Section: Discussionmentioning

confidence: 99%

SdrC induces staphylococcal biofilm formation through a homophilic interaction

Barbu

MacKenzie

Foster

et al. 2014

Molecular Microbiology

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“…Tjalsma et al, 2008, also tested trypsin-beads, which are unable to penetrate the bacterial cell-wall and thus probably ensure genuine surface-exposed localization [27]. The trypsin shaving approach has been mainly used thus far in combination with MS analysis for identification of potential vaccine candidates in pathogens such as Streptococcus pyogenes or Bacillus subtilis [29, 30], for characterization of S. aureus surfactome interactions with host plasma proteins [31], and for characterization of S. aureus adhesins or other surface proteins with adhesive functions [32]. …”

Section: Introductionmentioning

confidence: 99%

Changes in the Expression of Biofilm-Associated Surface Proteins inStaphylococcus aureusFood-Environmental Isolates Subjected to Sublethal Concentrations of Disinfectants

Cincarova

Polanský

Babák

et al. 2016

BioMed Research International

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Sublethal concentrations (sub-MICs) of certain disinfectants are no longer effective in removing biofilms from abiotic surfaces and can even promote the formation of biofilms. Bacterial cells can probably adapt to these low concentrations of disinfectants and defend themselves by way of biofilm formation. In this paper, we report on three Staphylococcus aureus biofilm formers (strong B+++, moderate B++, and weak B+) that were cultivated with sub-MICs of commonly used disinfectants, ethanol or chloramine T, and quantified using Syto9 green fluorogenic nucleic acid stain. We demonstrate that 1.25–2.5% ethanol and 2500 μg/mL chloramine T significantly enhanced S. aureus biofilm formation. To visualize differences in biofilm compactness between S. aureus biofilms in control medium, 1.25% ethanol, or 2500 μg/mL chloramine T, scanning electron microscopy was used. To describe changes in abundance of surface-exposed proteins in ethanol- or chloramine T-treated biofilms, surface proteins were prepared using a novel trypsin shaving approach and quantified after dimethyl labeling by LC-LTQ/Orbitrap MS. Our data show that some proteins with adhesive functions and others with cell maintenance functions and virulence factor EsxA were significantly upregulated by both treatments. In contrast, immunoglobulin-binding protein A was significantly downregulated for both disinfectants. Significant differences were observed in the effect of the two disinfectants on the expression of surface proteins including some adhesins, foldase protein PrsA, and two virulence factors.

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“…For this purpose, we performed in vitro cell surface ''shaving" experiments using C. difficile cells and recombinant PPEP-1 (rPPEP-1), in analogy to proteomic approaches which have been developed to study cell surface proteomes in general [26,27]. Following incubation of the C. difficile cells with rPPEP-1 for 1 h, cells were pelleted by centrifugation and the resulting supernatant analyzed for the presence of the CD2831 product peptide PAPPNTDEPIVNP.…”

Section: Cleavage Of Endogenous Cd2831 From Wt and Ct::ppep-1 Cellsmentioning

confidence: 99%

Clostridium difficile secreted Pro‐Pro endopeptidase PPEP‐1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831

et al. 2015

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a b s t r a c tThe Clostridium difficile cd2830 gene product is a secreted metalloprotease, named Pro-Pro endopeptidase (PPEP-1). PPEP-1 cleaves C. difficile cell surface proteins (e.g. CD2831). Here, we confirmed that PPEP-1 has a unique preference for prolines surrounding the scissile bond. Moreover, we show that it exhibits a high preference for an asparagine at the P2 position and hydrophobic residues at the P3 position. Using a PPEP-1 knockout C. difficile strain, we demonstrate that the removal of the collagen binding protein CD2831 is fully attributable to PPEP-1 activity. The PPEP-1 knockout strain demonstrated higher affinity for collagen type I with attenuated virulence in hamsters.

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Proteomic and Transcriptomic Profiling of Staphylococcus aureus Surface LPXTG-proteins: Correlation with agr Genotypes and Adherence Phenotypes

Cited by 38 publications

References 63 publications

SdrC induces staphylococcal biofilm formation through a homophilic interaction

SdrC induces staphylococcal biofilm formation through a homophilic interaction

Changes in the Expression of Biofilm-Associated Surface Proteins inStaphylococcus aureusFood-Environmental Isolates Subjected to Sublethal Concentrations of Disinfectants

Clostridium difficile secreted Pro‐Pro endopeptidase PPEP‐1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831

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