Identification of a Fibronectin Binding Protein from<i>Streptococcus mutans</i>

Chia, Jean-San; Yeh, Chiou-Yueh; Chen, Jen‐Yang

doi:10.1128/iai.68.4.1864-1870.2000

Cited by 36 publications

(36 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The capacity of C. difficile to bind immobilized fibronectin in vitro may translate to its capacity to bind to fibronectin present on the surface of numerous eukaryotic cells in vivo. Binding to soluble fibronectin, which is ubiquitous in body fluids, could allow the bacteria to attach directly to tissues (Chia et al, 2000). C. difficile may also be able to bind to tissues through fibronectin-fibrin, fibronectin-collagen or fibronectin-fibronectin interactions (Vercellotti et al, 1985).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Identification and characterization of a fibronectin-binding protein from Clostridium difficile

et al. 2003

View full text Add to dashboard Cite

A 68 kDa fibronectin-binding protein (Fbp68) from Clostridium difficile displaying significant homology to several established or putative Fbps from other bacteria was identified. The one-copy gene is highly conserved in C. difficile isolates. Fbp68 was expressed in Escherichia coli in fusion with glutathione S-transferase; the fusion protein and the native Fbp68 were purified. Immunoblot analysis and cell fractionation experiments revealed that Fbp68 is present on the surface of the bacteria. Far-immuno dot-blotting demonstrated that Fbp68 was capable of fixing fibronectin. Indirect immunofluorescence and ELISA were employed to demonstrate that C. difficile could bind both soluble and immobilized fibronectin. With competitive adherence inhibition assays it was shown that antibodies raised against Fbp68 partially inhibited attachment of C. difficile to fibronectin and Vero cells. Furthermore, Vero cells could fix purified membrane-immobilized Fbp68. Thus Fbp68 appears to be one of the several adhesins identified to date in C. difficile.

show abstract

Section: Discussionmentioning

confidence: 99%

“…The technique used to examine binding of C. difficile to immobilized fibronectin was a modification of the ELISA described by Chia et al (2000). The experimental part with C. difficile was carried out in anaerobic conditions.…”

Section: Binding Of C Difficile To Soluble and Immobilized Fibronectinmentioning

confidence: 99%

Identification and characterization of a fibronectin-binding protein from Clostridium difficile

et al. 2003

View full text Add to dashboard Cite

show abstract

“…Oral viridans streptococci are pathogens associated with infective endocarditis, and the binding abilities of these organisms to subendothelial matrix proteins including collagen, sialoproteins, fibronectin, and laminin, as well as blood-derived fibrinogen (fibrin), are regarded as potential virulence factors (Sommer et al, 1992;Sciotti et al, 1997;Chia et al, 2000;Beg et al, 2002;Takahashi et al, 2002). Although S. mutans was reported to be responsible for 8-18% of total streptococcal endocarditis (Ryd et al, 1996), and extracellular protein antigen I/II was reported to be involved in binding of S. mutans cells to extracellular matrix protein (Love et al, 2000;Beg et al, 2002), including collagen, it has often been questioned whether S. mutans is a true pathogen in endocarditis.…”

Section: Discussionmentioning

confidence: 99%

Streptococcus mutans Strains Harboring Collagen-binding Adhesin

Satō

Okamoto²,

Kagami³

et al. 2004

J Dent Res

105

101

View full text Add to dashboard Cite

A previously unidentified 120-kDa protein was detected in Streptococcus mutans strain Z1 and was involved in the cold-agglutination of the strain. We have identified the gene, designated cnm, as being involved in the agglutination of strain Z1 following random mutagenesis. The amino acid sequence of the deduced Cnm protein exhibited high similarity to those of collagen-binding adhesins from staphylococci and other organisms. To confirm whether the protein is involved in collagen-binding, we cloned a cnm gene fragment, overexpressed it in E.coli, and prepared crude extracts. The extracts containing recombinant protein exhibited binding to immobilized collagen and laminin but not to fibronectin. Compared with the parental strain Z1, the cold-agglutination-negative mutant 05A02 exhibited reduced binding to collagen and laminin but retained that to fibronectin. This gene was detected in some strains of S. mutans. Therefore, the cnm gene encoded a new strain-specific member of the collagen-binding adhesin family.

show abstract

“…There are two main forms of fibronectin, the secreted insoluble matrix protein and the soluble form present in plasma and extracellular fluids. Streptococci and staphylococci express various fibronectin binding adhesins [7,[10][11][12][13][14]. The binding of pathogenic Streptococcus pyogenes and Staphylococcus aureus to epithelial cells via fibronectin facilitates their entry into cells [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

“…These atypical fibronectin-binding proteins include FBP54 of S. pyogenes, PavA of S. pneumoniae, and FbpA of S. gordonii [7,10,19]. Chia et al observed that S. mutans cells could adsorb on their surface soluble fibronectin present in plasma [14]. Furthermore, these investigators demonstrated that S. mutans can bind soluble and immobilized fibronectin and identified a cell wall-associated protein, FBP-130, as a receptor that bound fibronectin.…”

Section: Introductionmentioning

confidence: 99%

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

View full text Add to dashboard Cite

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.

show abstract

Identification of a Fibronectin Binding Protein fromStreptococcus mutans

Cited by 36 publications

References 37 publications

Identification and characterization of a fibronectin-binding protein from Clostridium difficile

Identification and characterization of a fibronectin-binding protein from Clostridium difficile

Streptococcus mutans Strains Harboring Collagen-binding Adhesin

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

Contact Info

Product

Resources

About