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Infection and Immunity, October 1998, p. 4633-4639, Vol. 66, No. 10
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Binding Properties of Streptococcus gordonii SspA and SspB (Antigen I/II Family) Polypeptides Expressed on the Cell Surface of Lactococcus lactis MG1363

Ann R. Holmes,1 Christophe Gilbert,2 Jeremy M. Wells,2 and Howard F. Jenkinson3,*

Department of Oral Sciences and Orthodontics, University of Otago, Dunedin, New Zealand,1 and Department of Pathology, University of Cambridge, Cambridge CB2 1QP,2 and Department of Oral and Dental Science, University of Bristol, Bristol BS1 2LY,3 United Kingdom

Received 11 May 1998/Returned for modification 23 June 1998/Accepted 22 July 1998

The oral bacterium Streptococcus gordonii expresses two cell wall-associated polypeptides, designated SspA (1,542 amino acid residues) and SspB (1,462 amino acid residues), that have 70% sequence identity. These polypeptides are members of the antigen I/II family of oral streptococcal adhesins and mediate the binding of streptococci to salivary glycoproteins, collagen, and other oral microorganisms such as Actinomyces naeslundii. To determine if SspA and SspB have differential binding properties, the coding sequences of the sspA and sspB genes were cloned into expression plasmid vector pTREX1-usp45LS to generate pTREX1-sspA and pTREX1-sspB, respectively, and the Ssp polypeptides were displayed on the cell surface of Lactococcus lactis MG1363. Lactococcal cells expressing similar levels of surface SspA or SspB polypeptide were then compared for their abilities to adhere to a range of antigen I/II polypeptide substrates. More than twice as many L. lactis cells expressing SspA bound to immobilized salivary agglutinin glycoprotein (SAG) as did L. lactis cells expressing SspB. In contrast, lactococci expressing SspB adhered twice as well as lactococci producing SspA to collagen type I and to Candida albicans. The binding of A. naeslundii to lactococci was only weakly enhanced by surface expression of Ssp polypeptides. L. lactis(pTREX1-sspB) cells bound in greater numbers to SAG than did Enterococcus faecalis JH2-2 cells expressing SspB from pAM401EB-5. The results suggest that SspA and SspB have markedly different binding affinities for their oral substrates and thus may function to promote site diversity in colonization by S. gordonii.

* Corresponding author. Mailing address: Department of Oral and Dental Science, Division of Oral Medicine, Pathology and Microbiology, University of Bristol Dental School, Lower Maudlin St., Bristol BS1 2LY, United Kingdom. Phone: 44 117 928 4304. Fax: 44 117 428 4428. Email: howard.jenkinson{at}bristol.ac.uk.

Infection and Immunity, October 1998, p. 4633-4639, Vol. 66, No. 10
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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