Binding of the Streptococcal Surface Glycoproteins GspB and Hsa to Human Salivary Proteins

GspB and Hsa are homologous surface glycoproteins of Streptococcus gordonii that bind sialic acid moieties on platelet membrane glycoprotein Ib[alpha]. 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...

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Bibliographic Details
Published in:Infection and Immunity 2006-03, Vol.74 (3), p.1933-1940
Main Authors: Takamatsu, Daisuke, Bensing, Barbara A, Prakobphol, Akraporn, Fisher, Susan J, Sullam, Paul M
Format: Article
Language:English
Subjects:
Adhesins, Bacterial - metabolism
Bacterial Adhesion
Bacteriology
Biological and medical sciences
Carrier Proteins - metabolism
Fundamental and applied biological sciences. Psychology
Humans
Membrane Glycoproteins - metabolism
Microbiology
Miscellaneous
Molecular Pathogenesis
Salivary Proteins and Peptides - metabolism
Streptococcus - chemistry
Streptococcus gordonii
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Summary:GspB and Hsa are homologous surface glycoproteins of Streptococcus gordonii that bind sialic acid moieties on platelet membrane glycoprotein Ib[alpha]. 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.
ISSN:0019-9567
1098-5522
DOI:10.1128/IAI.74.3.1933-1940.2006