This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chia, J.-S.
Right arrow Articles by Chen, J.-Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chia, J.-S.
Right arrow Articles by Chen, J.-Y.

 Previous Article  |  Next Article 

Infection and Immunity, April 2000, p. 1864-1870, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Identification of a Fibronectin Binding Protein from Streptococcus mutans

Jean-San Chia,* Chiou-Yueh Yeh, and Jen-Yang Chen

Graduate Institute of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan, Republic of China

Received 27 October 1999/Returned for modification 22 November 1999/Accepted 14 December 1999

The interaction of viridans streptococci with components of the extracellular matrix (ECM) plays an important role in the pathogenesis of infective endocarditis. We have identified a surface protein of Streptococcus mutans which binds the ECM constituent fibronectin (Fn). Initially, we found that S. mutans could adsorb soluble Fn in plasma, but with lower efficiency than Streptococcus pyogenes. In addition, S. mutans could bind immobilized Fn in a dose-dependent manner when tested using an enzyme-linked immunosorbent assay. Crude extracts of cell wall-associated proteins or extracellular proteins from S. mutans MT8148 specifically bound Fn through a protein with the molecular mass of ca. 130 kDa, as detected by far-Western immunoblotting. The candidate Fn binding protein (FBP-130) was purified to near homogeneity by using Fn coupled Sepharose 4B affinity column chromatography. A rabbit polyclonal antibody against FBP-130 reacted specifically with a protein of molecular mass of ca. 130 kDa in both cell wall and extracellular fractions, and the abundance of FBP was higher in the former than in the latter fractions. The purified FBP bound specifically to immobilized Fn, whereas the binding of soluble Fn to coated FBP could only be detected in the presence of high concentrations of Fn. The purified FBP, as well as anti-FBP immunoglobulin G, inhibited the adherence of S. mutans to immobilized Fn and endothelial cells (ECV304) in a dose-dependent manner. These results demonstrated that FBP-130 mediated the adherence of S. mutans specifically to Fn and endothelial cells in vitro. The characteristics of S. mutans and FBP-130 in binding Fn confirmed that viridans streptococci adopt different strategies in their interaction with ECM.

* Corresponding author. Mailing address: No. 1, Jen Ai Road 1st Section, Rm. 713, Graduate Institute of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan. Phone: 886-2-23970800, ext. 8222. Fax: 886-2-23915293. E-mail: chiajs{at}ha.mc.edu.tw.

Infection and Immunity, April 2000, p. 1864-1870, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Sato, Y., Okamoto, K., Kagami, A., Yamamoto, Y., Igarashi, T., Kizaki, H. (2004). Streptococcus mutans Strains Harboring Collagen-binding Adhesin. JDR 83: 534-539 [Abstract] [Full Text]  
  • Chia, J.-S., Lin, Y.-L., Lien, H.-T., Chen, J.-Y. (2004). Platelet Aggregation Induced by Serotype Polysaccharides from Streptococcus mutans. Infect. Immun. 72: 2605-2617 [Abstract] [Full Text]  
  • Hennequin, C., Janoir, C., Barc, M.-C., Collignon, A., Karjalainen, T. (2003). Identification and characterization of a fibronectin-binding protein from Clostridium difficile. Microbiology 149: 2779-2787 [Abstract] [Full Text]  
  • Ajdic', D., McShan, W. M., McLaughlin, R. E., Savic', G., Chang, J., Carson, M. B., Primeaux, C., Tian, R., Kenton, S., Jia, H., Lin, S., Qian, Y., Li, S., Zhu, H., Najar, F., Lai, H., White, J., Roe, B. A., Ferretti, J. J. (2002). Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen. Proc. Natl. Acad. Sci. USA 99: 14434-14439 [Abstract] [Full Text]  
  • de Greeff, A., Buys, H., Verhaar, R., Dijkstra, J., van Alphen, L., Smith, H. E. (2002). Contribution of Fibronectin-Binding Protein to Pathogenesis of Streptococcus suis Serotype 2. Infect. Immun. 70: 1319-1325 [Abstract] [Full Text]  
  • Petersen, F. C., Assev, S., van der Mei, H. C., Busscher, H. J., Scheie, A. A. (2002). Functional Variation of the Antigen I/II Surface Protein in Streptococcus mutans and Streptococcus intermedius. Infect. Immun. 70: 249-256 [Abstract] [Full Text]  
  • Honma, K., Kuramitsu, H. K., Genco, R. J., Sharma, A. (2001). Development of a Gene Inactivation System for Bacteroides forsythus: Construction and Characterization of a BspA Mutant. Infect. Immun. 69: 4686-4690 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»