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Infection and Immunity, November 2004, p. 6748-6752, Vol. 72, No. 11
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.11.6748-6752.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Streptococcus mutans Surface {alpha}-Enolase Binds Salivary Mucin MG2 and Human Plasminogen

Jingping Ge,1 Diana M. Catt,2 and Richard L. Gregory1,2*

Department of Pathology and Laboratory Medicine, School of Medicine,1 Department of Oral Biology, School of Dentistry, Indiana University, Indianapolis, Indiana2

Received 24 February 2004/ Returned for modification 31 March 2004/ Accepted 28 July 2004

Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis identified enolase as a cell surface component of Streptococcus mutans, which was confirmed by enzyme-linked immunosorbent assay, Western blotting, and transmission electron microscopy. Surface enolase was demonstrated to bind to human plasminogen and salivary mucin MG2. The results suggested a role for enolase in S. mutans attachment, clearance, or breach of the bloodstream barrier.

* Corresponding author. Mailing address: Department of Oral Biology, Indiana University School of Dentistry, 1121 West Michigan St., Indianapolis, IN 46202. Phone: (317) 274-9949. Fax: (317) 278-1411. E-mail: rgregory{at}iupui.edu.

Editor: J. B. Bliska

Infection and Immunity, November 2004, p. 6748-6752, Vol. 72, No. 11
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.11.6748-6752.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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