Binding of Streptococcus mutans to extracellular matrix molecules and fibrinogen

Beg, Anjum M; Jones, Micheala N.; Miller-Torbert, Tracey A.; Holt, Robert G.

doi:10.1016/s0006-291x(02)02390-2

Cited by 66 publications

(65 citation statements)

References 16 publications

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“…Moreover, continuous detections of this bacterium in specimens from patients suffering from such disease emphasize the importance of S. mutans in IE (Gauduchon et al, 2001;Nomura et al, 2006;Vose et al, 1987;Ullman et al, 1988). Indeed, studies to clarify specific components involved in IE in S. mutans have also been performed worldwide (Beg et al, 2002;Jung et al, 2009; MatsumotoNakano et al, 2009;Miller-Torbert et al, 2008).IE is initiated by the binding of bacterial surface molecules to host extracellular matrix (ECM) proteins exposed on damaged heart tissue (Moreillon & Que, 2004). In S. mutans, collagen-binding adhesin or Cnm protein, encoded by the cnm gene, was reported as a strain-specific collagen-binding molecule (Sato et al, 2004).…”

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confidence: 99%

Multilocus sequence typing analysis of Streptococcus mutans strains with the cnm gene encoding collagen-binding adhesin

Lapirattanakul

Nakano

Nomura

et al. 2011

Journal of Medical Microbiology

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Streptococcus mutans is one of the oral pathogens associated with infective endocarditis (IE).With respect to bacterial binding ability to the extracellular matrix, the Cnm protein, a cell surface collagen-binding adhesin of S. mutans, is known as one of the possible virulence factors with regard to IE. In this study, we aimed to determine the distribution of the cnm gene, which encodes Cnm, in a large number of clinical isolates of S. mutans from Thai subjects. Then, the cnm-positive strains were classified using a multilocus sequence typing (MLST) scheme, which we constructed previously. In addition, the data were analysed together with our previous MLST data of cnmpositive strains from Japan and Finland in order to evaluate the clonal relationship among S. mutans strains harbouring the cnm gene. The cnm gene was detected in 12.4 % of all 750 Thai isolates, and serotype f showed the highest rate of detection (54.5 %). According to the MLST data, two clonal complex groups were revealed as the important clones related to cnm-positive S. mutans from various origins of isolation. Moreover, the collagen-binding properties of S. mutans strains with the cnm gene were significantly greater than those of strains without the gene, although four cnm-negative strains classified into two sequence types (STs), ST110 and ST136, showed extremely high collagen-binding rates suggesting the presence of additional genes involved with collagen binding in these STs. Taken together, these results provided information on both epidemiological as well as evolutional aspects of S. mutans possessing the cnm gene. INTRODUCTIONStreptococcus mutans is a well-known pathogen of dental caries (Hamada & Slade, 1980), which consists of four serotypes, c, e, f and k (Linzer et al., 1986;). The detection rate of serotype c is highest among the strains isolated from oral cavities, followed by serotype e, while serotypes f and k are regarded as being present in minor proportions . Various pieces of evidence show the association of S. mutans with some life-threatening diseases such as infective endocarditis (IE), although the major species related to IE belong to the mitis group of oral streptococci (Banas, 2004;Mylonakis & Calderwood, 2001). Moreover, continuous detections of this bacterium in specimens from patients suffering from such disease emphasize the importance of S. mutans in IE (Gauduchon et al., 2001;Nomura et al., 2006;Vose et al., 1987;Ullman et al., 1988). Indeed, studies to clarify specific components involved in IE in S. mutans have also been performed worldwide (Beg et al., 2002;Jung et al., 2009; MatsumotoNakano et al., 2009;Miller-Torbert et al., 2008).IE is initiated by the binding of bacterial surface molecules to host extracellular matrix (ECM) proteins exposed on damaged heart tissue (Moreillon & Que, 2004). In S. mutans, collagen-binding adhesin or Cnm protein, encoded by the cnm gene, was reported as a strain-specific collagen-binding molecule (Sato et al., 2004). The Cnm protein possesses a collagen-binding domain (CBD) in ...

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confidence: 99%

Multilocus sequence typing analysis of Streptococcus mutans strains with the cnm gene encoding collagen-binding adhesin

Lapirattanakul

Nakano

Nomura

et al. 2011

Journal of Medical Microbiology

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“…A study by Sciotti et al reported that the N-terminal region of antigen I/II bound to various extracellular matrix proteins such as, fibronectin, laminin and collagen [23]. Our laboratory has compared the ability of parental strain, S. mutans NG8, and its isogenic antigen I/II-deficient mutant strain, 834, to bind fibronectin [9]. We find that the mutant NG8 strain demonstrated a decreased adherence to immobilized fibronectin.…”

Section: Discussionmentioning

confidence: 75%

“…mutans M51 has a spontaneously generated streptomycin-resistance phenotype and was obtained from the Centers for Disease Control and Prevention and was isolated from the peripheral blood of a patient clinically diagnosed with infective endocarditis [9]. The isogenic mutant of S. mutans M51, ΔSmFnB, was constructed by allelic exchange and has a deficiency in the expression of the SmFnB protein.…”

Section: Bacterial Strains and Mediamentioning

confidence: 99%

“…The plates were developed with the chromogenic substrate tetramethylbenzidine and the absorbance read at 450 nm. The ELISA technique previously described was used to measure the comparative ability of wild-type S. mutans M51 and the isogenic strain with the mutated gene for the fibronectin-binding protein to bind to fibronectin [9]. Clustal W sequence alignment of the translated protein sequences of S. mutans (SmFnB), S. gordonii (FbpA), and S. pyogenes (FBP54) fibronectin-binding proteins.…”

Section: Fibronectin-binding Assaysmentioning

confidence: 99%

“…Since the oral bacteria that cause chronic infective endocarditis primarily adhere to damaged heart tissue, it is believed that extracellular matrix molecules act as receptors for bacterial attachment. Previous studies have shown that a number of species of bacteria, including S. mutans, adhere to certain extracellular matrix proteins such as, fibronectin, laminin, collagen, and the blood clotting component, fibrinogen [3][4][5][6][7][8][9]. Fibronectin is a 440 kDa dimeric glycoprotein that is a common substrate for the attachment of bacteria to the host cell surface.…”

Section: Introductionmentioning

confidence: 99%

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Inactivation of a gene for a fibronectin-binding protein of the oral bacterium Streptococcus mutans partially impairs its adherence to fibronectin

Miller-Torbert

Sharma

Holt

2008

Microbial Pathogenesis

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A sequence of 1,647 base pairs in length of S. mutans DNA that encodes for a 63 kDa protein with significant amino acid similarity with fibronectin-binding proteins of S. pyogenes and S. gordonii was cloned. The putative recombinant fibronectin-binding protein of S. mutans was purified using affinity chromatography and the cloned protein was used to prepare polyclonal antibodies against the recombinant protein. In immunoblot assays, antibodies against the S. pyogenes fibronectinbinding protein, FBP54, were cross-reactive with the S. mutans protein that was designated SmFnB. Additionally, antibodies to the S. mutans SmFnB protein reacted with the S. pyogenes FBP54 protein.The S. mutans SmFnB protein was found to bind to immobilized fibronectin in a concentration dependant manner. A mutant strain of S. mutans M51 that was constructed by alleleic exchange did not express the SmFnB protein. This mutant strain, S. mutans ΔSmFnB, was determined in an ELISA to bind to immobilized fibronectin 30% less when compared to the parental strain S. mutans M51. The results are consistent with the conclusion that the 63 kDa SmFnB protein of S. mutans is a fibronectin-binding protein that may contribute to the interaction of S. mutans with damaged heart tissue during pathogenesis of infective endocarditis. Also, the study suggests that multiple molecules may mediate the interaction of S. mutans with fibronectin.

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A mariner transposon vector adapted for mutagenesis in oral streptococci

et al. 2014

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This article describes the construction and characterization of a mariner-based transposon vector designed for use in oral streptococci, but with a potential use in other Gram-positive bacteria. The new transposon vector, termed pMN100, contains the temperature-sensitive origin of replication repATs-pWV01, a selectable kanamycin resistance gene, a Himar1 transposase gene regulated by a xylose-inducible promoter, and an erythromycin resistance gene flanked by himar inverted repeats. The pMN100 plasmid was transformed into Streptococcus mutans UA159 and transposon mutagenesis was performed via a protocol established to perform high numbers of separate transpositions despite a low frequency of transposition. The distribution of transposon inserts in 30 randomly picked mutants suggested that mariner transposon mutagenesis is unbiased in S. mutans. A generated transposon mutant library containing 5000 mutants was used in a screen to identify genes involved in the production of sucrose-dependent extracellular matrix components. Mutants with transposon inserts in genes encoding glycosyltransferases and the competence-related secretory locus were predominantly found in this screen.

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Binding of Streptococcus mutans to extracellular matrix molecules and fibrinogen

Cited by 66 publications

References 16 publications

Multilocus sequence typing analysis of Streptococcus mutans strains with the cnm gene encoding collagen-binding adhesin

Multilocus sequence typing analysis of Streptococcus mutans strains with the cnm gene encoding collagen-binding adhesin

Inactivation of a gene for a fibronectin-binding protein of the oral bacterium Streptococcus mutans partially impairs its adherence to fibronectin

A mariner transposon vector adapted for mutagenesis in oral streptococci

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