2004
DOI: 10.1016/j.febslet.2004.04.029
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Streptococcal antigen I/II binds to extracellular proteins through intermolecular β‐sheets

Abstract: One of the functions associated with the oral streptococcal surface protein I/II is to bind to human extracellular matrix molecules or blood components, which could act as opportunistic ligands in pathological circumstances. In order to understand the relative specificity of the binding repertoire of this bacterial adhesin, we examined by infrared measurements the mode of binding of the protein I/II from Streptococcus mutans OMZ175 (I/IIf) to fibronectin and fibrinogen. This approach revealed the beta-structur… Show more

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Cited by 12 publications
(7 citation statements)
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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%
“…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%
“…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%
“…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. 2,4,5,1923 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%