Binding of oral streptococci to human fibrinogen

Lee, S. Y.; Kim, K.-K.; Choe, Son-Jin

doi:10.1034/j.1399-302x.2001.016002088.x

Cited by 15 publications

(12 citation statements)

References 46 publications

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“…In contrast, S. oralis , which is as common as S. sanguinis (Douglas et al , 1993) in infective endocarditis, has no direct affinity for platelets, and so we speculate that this organism colonizes vegetations by means of recognition of one or more matrix proteins present (e.g. fibrin, fibronectin; Lee et al , 2001). Of course, such binding may also contribute to S. gordonii and S. sanguinis colonization.…”

Section: Discussionmentioning

confidence: 90%

Relationship between the ability of oral streptococci to interact with platelet glycoprotein IbÎ± and with the salivary low-molecular-weight mucin, MG2

Plummer¹,

Douglas²

2006

FEMS Immunology &Amp; Medical Microbiology

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The oral streptococci Streptococcus sanguinis, Streptococcus gordonii and Streptococcus oralis are common aetiological agents of infective endocarditis, and their ability to adhere to and induce the aggregation of platelets is thought to be a virulence trait. The platelet glycoprotein GPIbalpha has been implicated as the adhesion receptor for S. sanguinis and S. gordonii, but it is not known if this is the case for S. oralis and other species. The aim of this study was to determine the GPIbalpha-interactive capability of a range of oral streptococci and to determine the relationship between this capability and their ability to interact with the salivary constituents that they would encounter in their normal habitat. All platelet-adhesive S. sanguinis strains and most S. gordonii strains adhered in a GPIbalpha-dependent manner, but strains of S. oralis, Streptococcus cristatus, Streptococcus parasanguinis and Streptococcus mitis had no direct affinity for platelets. Those strains that were able to bind GPIbalpha also bound to the low-molecular-weight submandibular salivary mucin, MG2, and this interaction was sialic acid-dependent. The data suggest that S. sanguinis and S. gordonii may be efficient colonizers of platelet vegetations because of their adaptation to recognize sialylated salivary mucins. In contrast, S. oralis does not interact with platelets and so is likely to colonize vegetations through an as yet unidentified mechanism.

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Section: Discussionmentioning

confidence: 90%

Relationship between the ability of oral streptococci to interact with platelet glycoprotein IbÎ± and with the salivary low-molecular-weight mucin, MG2

Plummer¹,

Douglas²

2006

FEMS Immunology &Amp; Medical Microbiology

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“…For example, Group A and G streptococci can bind both soluble and immobilized forms of fibrinogen, whereas several oral streptococci appear to bind only immobilized fibrinogen [27], [28], [29]. To assess whether fibrinogen binding by lysin SM1 was phase-dependent, we reversed the binding conditions, such that FLAG lysin SM1 , untagged lysin SM1 , and FLAG AP (all at 10 µg/ml) were immobilized in microtiter wells, and probed with the increasing concentration of fibrinogen in solution.…”

Section: Resultsmentioning

confidence: 99%

Bacteriophage Lysin Mediates the Binding of Streptococcus mitis to Human Platelets through Interaction with Fibrinogen

et al. 2010

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The binding of bacteria to human platelets is a likely central mechanism in the pathogenesis of infective endocarditis. We have previously found that platelet binding by Streptococcus mitis SF100 is mediated by surface components encoded by a lysogenic bacteriophage, SM1. We now demonstrate that SM1-encoded lysin contributes to platelet binding via its direct interaction with fibrinogen. Far Western blotting of platelets revealed that fibrinogen was the major membrane-associated protein bound by lysin. Analysis of lysin binding with purified fibrinogen in vitro confirmed that these proteins could bind directly, and that this interaction was both saturable and inhibitable. Lysin bound both the Aα and Bβ chains of fibrinogen, but not the γ subunit. Binding of lysin to the Bβ chain was further localized to a region within the fibrinogen D fragment. Disruption of the SF100 lysin gene resulted in an 83±3.1% reduction (mean ± SD) in binding to immobilized fibrinogen by this mutant strain (PS1006). Preincubation of this isogenic mutant with purified lysin restored fibrinogen binding to wild type levels. When tested in a co-infection model of endocarditis, loss of lysin expression resulted in a significant reduction in virulence, as measured by achievable bacterial densities (CFU/g) within vegetations, kidneys, and spleens. These results indicate that bacteriophage-encoded lysin is a multifunctional protein, representing a new class of fibrinogen-binding proteins. Lysin appears to be cell wall-associated through its interaction with choline. Once on the bacterial surface, lysin can bind fibrinogen directly, which appears to be an important interaction for the pathogenesis of endocarditis.

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“…Subsequent opportunistic introduction of the bacteria through the circulation allows dissemination to extra-oral sites via interaction of these streptococci with extracellular matrix molecules or blood components which function as cell receptors for these bacteria [1][2][3][4][5]. Subsequent opportunistic introduction of the bacteria through the circulation allows dissemination to extra-oral sites via interaction of these streptococci with extracellular matrix molecules or blood components which function as cell receptors for these bacteria [1][2][3][4][5].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2004

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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-structure forming capacity of I/IIf upon interaction with both proteins. The forming of intermolecular beta-structures may provide a non-selective way of interaction between I/IIf and its possible targets.

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Binding of oral streptococci to human fibrinogen

Cited by 15 publications

References 46 publications

Relationship between the ability of oral streptococci to interact with platelet glycoprotein IbÎ± and with the salivary low-molecular-weight mucin, MG2

Relationship between the ability of oral streptococci to interact with platelet glycoprotein IbÎ± and with the salivary low-molecular-weight mucin, MG2

Bacteriophage Lysin Mediates the Binding of Streptococcus mitis to Human Platelets through Interaction with Fibrinogen

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

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