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Infection and Immunity, September 2001, p. 5736-5741, Vol. 69, No. 9
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.9.5736-5741.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Discrete Protein Determinant Directs the Species-Specific Adherence of Porphyromonas gingivalis to Oral Streptococci

Donald R. Demuth,1,* Douglas C. Irvine,1 J. W. Costerton,2 Guy S. Cook,3 and Richard J. Lamont4

Department of Biochemistry, University of Pennsylvania School of Dental Medicine, Philadelphia, Pennsylvania 191041; Center for Biofilm Engineering, Montana State University,3 and Bacterin, Inc.,4 Bozeman, Montana 59717; and Department of Oral Biology, University of Washington, Seattle, Washington 981952

Received 31 January 2001/Returned for modification 4 April 2001/Accepted 1 June 2001

For pathogens to survive in the human oral cavity, they must identify a suitable niche in the complex multispecies biofilm that exists on oral tissues. The periodontal pathogen Porphyromonas gingivalis adheres to Streptococcus gordonii by interacting with a specific region of the streptococcal SspB polypeptide, designated BAR. However, it does not adhere to Streptococcus mutans, which expresses SpaP, a highly conserved homolog of SspB. Comparison of the predicted secondary structure of BAR with the corresponding region of SpaP suggested that the substitution of Asn for Gly1182 and Val for Pro1185 in SspB may confer a unique local structure that is not conserved in SpaP. A synthetic peptide of 26 amino acids that encompassed residues 1167 to 1193 of SspB promoted avid adherence of P. gingivalis, whereas a peptide derived from the region corresponding to BAR in SpaP was inactive. Substitution of Gly1182 and Pro1185 for Asn1182 and Val1185 in SspB by site-specific mutation generated proteins that were predicted to assume an SpaP-like secondary structure, and the purified proteins did not promote P. gingivalis adherence. Furthermore, Enterococcus faecalis strains expressing the site-specific mutants did not support adherence of P. gingivalis cells. In contrast, P. gingivalis adhered efficiently to E. faecalis strains expressing intact SspB or SspB-SpaP chimeric proteins containing BAR. These results suggest that a region of SspB consisting of 26 amino acids is sufficient to mediate the adherence of P. gingivalis to S. gordonii and that the species specificity of adherence arises from its interaction with a discrete structural determinant of SspB that is not conserved in SpaP.

* Corresponding author. Mailing address: Department of Biochemistry, Levy Research Bldg., Room 540, University of Pennsylvania School of Dental Medicine, 4010 Locust Street, Philadelphia, PA 19104-6002. Phone: (215) 898-2125. Fax: (215) 898-3695. E-mail: demuth{at}biochem.dental.upenn.edu.

Infection and Immunity, September 2001, p. 5736-5741, Vol. 69, No. 9
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.9.5736-5741.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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