Binding of the Streptococcal Surface Glycoproteins GspB and Hsa to Human Salivary Proteins
- Daisuke Takamatsu1,2,†,
- Barbara A. Bensing1,2,
- Akraporn Prakobphol3,
- Susan J. Fisher3,4 and
- Paul M. Sullam1,2,*
GspB and Hsa are homologous surface glycoproteins of Streptococcus gordonii that bind sialic acid moieties on platelet membrane glycoprotein Ibα. Since this species is an important member of the oral flora, we examined the direct binding of these adhesins to human salivary proteins. Both GspB and Hsa bound low-molecular-weight salivary mucin MG2 and salivary agglutinin. Hsa also bound several other salivary proteins, including secretory immunoglobulin A. Screening of six oral streptococcal isolates revealed that at least two of the strains expressed GspB homologues. These results indicate that GspB-like adhesins may be important for oral bacterial colonization.
- Received 21 November 2005.
- Returned for modification 9 December 2005.
- Accepted 19 December 2005.
- ↵*Corresponding author. Mailing address: Division of Infectious Diseases, VA Medical Center (111W), 4150 Clement Street, San Francisco, CA 94121. Phone: (415) 221-4810, ext. 2550. Fax: (415) 750-0502. E-mail: .
↵† Present address: Molecular Bacteriology Section, Department of Infectious Diseases, National Institute of Animal Health, 3-1-5 Kannondai, Tsukuba, Ibaraki 305-0856, Japan.
Editor: J. N. Weiser
- American Society for Microbiology