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Structure, function and immunogenicity of streptococcal antigen I/II polypeptides
Author(s) -
Jenkinson Howard F.,
Demuth Donald R.
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1997.2021577.x
Subject(s) - biology , immunogenicity , microbiology and biotechnology , antigen , streptococcus , function (biology) , computational biology , virology , immunology , bacteria , genetics
The antigen I/II family of cell‐surface‐anchored polypeptides in oral streptococci are structurally complex multi‐functional adhesins, with multiple ligand‐binding sites. Discrete regions within these polypeptides bind human salivary glycoproteins, other microbial cells, and calcium. Sequences within the N‐terminal region bind preferentially fluid‐phase glycoproteins, while the C‐terminal half of the polypeptide contains species‐specific adhesion‐mediating sequences that bind surface‐immobilized glycoproteins. These features may assist streptococcal adhesion to oral surface receptors despite the presence of excess fluid‐phase receptors. Immunological studies reveal an array of T‐cell and B‐cell epitopes presented by antigen I/II polypeptides and suggest the occurrence of natural suppression of human antibodies to the adhesion‐mediating sequences. The functional and immunological properties of antigen I/II proteins may account to a major extent for the success of oral streptococci colonizing and surviving within the human host.