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Infection and Immunity, July 2005, p. 3983-3989, Vol. 73, No. 7
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.7.3983-3989.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Short Fimbriae of Porphyromonas gingivalis and Their Role in Coadhesion with Streptococcus gordonii

Yoonsuk Park,1 M. Regina Simionato,1,2 Kachiko Sekiya,3 Yukitaka Murakami,4 Deanna James,5 Weibin Chen,6 Murray Hackett,6 Fuminobu Yoshimura,4 Donald R. Demuth,5 and Richard J. Lamont1*

Department of Oral Biology, University of Florida, Gainesville, Florida 32610,1 Department of Microbiology, Institute of Biomedical Sciences, University of Sao Paulo, Sao Paulo, Brazil,2 School of Pharmaceutical Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo 108-8641, Japan,3 Department of Microbiology, Aichi-Gakuin University, 1-100 Kusumoto-cho, Chikusa-ku, Nagoya 464-8650, Japan,4 Department of Medicinal Chemistry, University of Washington, Seattle, Washington 98195,5 Department of Periodontology and Dental Hygiene, University of Louisville, Louisville, Kentucky 402926

Received 22 September 2004/ Returned for modification 27 December 2004/ Accepted 24 February 2005

Porphyromonas gingivalis, one of the causative agents of adult periodontitis, attaches and forms biofilms on substrata of Streptococcus gordonii. Coadhesion and biofilm development between these organisms requires the interaction of the short fimbriae of P. gingivalis with the SspB streptococcal surface polypeptide. In this study we investigated the structure and binding activities of the short fimbriae of P. gingivalis. Electron microscopy showed that isolated short fimbriae have an average length of 103 nm and exhibit a helical structure with a pitch of ca. 27 nm. Mfa1, the major protein subunit of the short fimbriae, bound to SspB protein, and this reaction was inhibited by purified recombinant Mfa1 and monospecifc anti-Mfa1 serum in a dose-dependent manner. Complementation of a polar Mfa1 mutant with the mfa1 gene restored the coadhesion phenotype of P. gingivalis. Hence, the Mfa1 structural fimbrial subunit does not require accessory proteins for binding to SspB. Furthermore, the interaction of Mfa1 with SspB is necessary for optimal coadhesion between P. gingivalis and S. gordonii.

* Corresponding author. Mailing address: Department of Oral Biology, College of Dentistry, University of Florida, Box 100424, Gainesville, FL 32610. Phone: (352) 392-5067. Fax: (352) 392-2361. E-mail: rlamont{at}dental.ufl.edu.

Editor: V. J. DiRita

Infection and Immunity, July 2005, p. 3983-3989, Vol. 73, No. 7
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.7.3983-3989.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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