Streptococcal antigen I/II binds to extracellular proteins through intermolecular β‐sheets

Kelemen, Lóránd; Rizk, Samer; Debreczeny, Mónika; Ogier, Joëlle; Szalontai, Balázs

doi:10.1016/j.febslet.2004.04.029

Cited by 12 publications

(7 citation statements)

References 26 publications

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“…While S. mutans could not mediate the conversion of fibrinogen into fibrin, it possessed a fibrinogen-binding activity. This is in agreement with previous studies reporting that the major surface antigen I/II of S. mutans is involved in the fibrinogen-binding activity [17, 18]. This property may allow bacteria to attach to each other through fibrinogen-mediated crossbridging.…”

Section: Discussionsupporting

confidence: 93%

Fibrinogen-InducedStreptococcus mutansBiofilm Formation and Adherence to Endothelial Cells

Bedran

Azelmat

Spolidório

et al. 2013

BioMed Research International

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Streptococcus mutans, the predominant bacterial species associated with dental caries, can enter the bloodstream and cause infective endocarditis. The aim of this study was to investigate S. mutans biofilm formation and adherence to endothelial cells induced by human fibrinogen. The putative mechanism by which biofilm formation is induced as well as the impact of fibrinogen on S. mutans resistance to penicillin was also evaluated. Bovine plasma dose dependently induced biofilm formation by S. mutans. Of the various plasma proteins tested, only fibrinogen promoted the formation of biofilm in a dose-dependent manner. Scanning electron microscopy observations revealed the presence of complex aggregates of bacterial cells firmly attached to the polystyrene support. S. mutans in biofilms induced by the presence of fibrinogen was markedly resistant to the bactericidal effect of penicillin. Fibrinogen also significantly increased the adherence of S. mutans to endothelial cells. Neither S. mutans cells nor culture supernatants converted fibrinogen into fibrin. However, fibrinogen is specifically bound to the cell surface of S. mutans and may act as a bridging molecule to mediate biofilm formation. In conclusion, our study identified a new mechanism promoting S. mutans biofilm formation and adherence to endothelial cells which may contribute to infective endocarditis.

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Section: Discussionsupporting

confidence: 93%

Fibrinogen-InducedStreptococcus mutansBiofilm Formation and Adherence to Endothelial Cells

Bedran

Azelmat

Spolidório

et al. 2013

BioMed Research International

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“…Although S. mutans has been reported to bind to ECM components, e.g. fibronectin through surface antigen I/II SpaP [58], [59], to the cell wall associated protein WapA [60], [61], the PavA-like protein (SMU. 1449) [2], and AtlA [62], none of these experiments was carried out using the UA159 strain.…”

Section: Resultsmentioning

confidence: 99%

Lack of the Delta Subunit of RNA Polymerase Increases Virulence Related Traits of Streptococcus mutans

et al. 2011

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The delta subunit of the RNA polymerase, RpoE, maintains the transcriptional specificity in Gram-positive bacteria. Lack of RpoE results in massive changes in the transcriptome of the human dental caries pathogen Streptococcus mutans. In this study, we analyzed traits of the ΔrpoE mutant which are important for biofilm formation and interaction with oral microorganisms and human cells and performed a global phenotypic analysis of its physiological functions. The ΔrpoE mutant showed higher self-aggregation compared to the wild type and coaggregated with other oral bacteria and Candida albicans. It formed a biofilm with a different matrix structure and an altered surface attachment. The amount of the cell surface antigens I/II SpaP and the glucosyltransferase GtfB was reduced. The ΔrpoE mutant displayed significantly stronger adhesion to human extracellular matrix components, especially to fibronectin, than the wild type. Its adhesion to human epithelial cells HEp-2 was reduced, probably due to the highly aggregated cell mass. The analysis of 1248 physiological traits using phenotype microarrays showed that the ΔrpoE mutant metabolized a wider spectrum of carbon sources than the wild type and had acquired resistance to antibiotics and inhibitory compounds with various modes of action. The reduced antigenicity, increased aggregation, adherence to fibronection, broader substrate spectrum and increased resistance to antibiotics of the ΔrpoE mutant reveal the physiological potential of S. mutans and show that some of its virulence related traits are increased.

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“…17,18 In the oral environment, P1 interacts primarily with the glycoprotein salivary agglutinin (SAG) complex predominantly composed of the scavenger receptor glycoprotein 340 (gp340/DMBT1), contained within the salivary pellicle on tooth surfaces. 2,4,5,19–23 P1 has also been shown to bind to extracellular matrix proteins such as collagen (Coll) 24–27 and fibronectin (Fn), 26,28,29 and is involved in cell–cell adhesion as well. 30 The ability of P1 to promote bacterial adherence and to affect colonization, cariogenicity and biofilm formation has made it of interest as a therapeutic target.…”

mentioning

confidence: 99%

Binding Forces of Streptococcus mutans P1 Adhesin

Sullan

Crowley

et al. 2015

ACS Nano

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Streptococcus mutans is a Gram-positive oral bacterium that is a primary etiological agent associated with human dental caries. In the oral cavity, S. mutans adheres to immobilized salivary agglutinin (SAG) contained within the salivary pellicle on the tooth surface. Binding to SAG is mediated by cell surface P1, a multifunctional adhesin that is also capable of interacting with extracellular matrix proteins. This may be of particular importance outside of the oral cavity as S. mutans has been associated with infective endocarditis and detected in atherosclerotic plaque. Despite the biomedical importance of P1, its binding mechanisms are not completely understood. In this work, we use atomic force microscopy-based single-molecule and single-cell force spectroscopy to quantify the nanoscale forces driving P1-mediated adhesion. Single-molecule experiments show that full-length P1, as well as fragments containing only the P1 globular head or C-terminal region, binds to SAG with relatively weak forces (~50 pN). In contrast, single-cell analyses reveal that adhesion of a single S. mutans cell to SAG is mediated by strong (~500 pN) and long-range (up to 6000 nm) forces. This is likely due to the binding of multiple P1 adhesins to self-associated gp340 glycoproteins. Such a cooperative, long-range character of the S. mutans–SAG interaction would therefore dramatically increase the strength and duration of cell adhesion. We also demonstrate, at single-molecule and single-cell levels, the interaction of P1 with fibronectin and collagen, as well as with hydrophobic, but not hydrophilic, substrates. The binding mechanism (strong forces, cooperativity, broad specificity) of P1 provides a molecular basis for its multifunctional adhesion properties. Our methodology represents a valuable approach to probe the binding forces of bacterial adhesins and offers a tractable methodology to assess anti-adhesion therapy.

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Streptococcal antigen I/II binds to extracellular proteins through intermolecular β‐sheets

Cited by 12 publications

References 26 publications

Fibrinogen-InducedStreptococcus mutansBiofilm Formation and Adherence to Endothelial Cells

Fibrinogen-InducedStreptococcus mutansBiofilm Formation and Adherence to Endothelial Cells

Lack of the Delta Subunit of RNA Polymerase Increases Virulence Related Traits of Streptococcus mutans

Binding Forces of Streptococcus mutans P1 Adhesin

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