Structure, function and immunogenicity of streptococcal antigen I/II polypeptides

被引:175
作者
Jenkinson, HF [1 ]
Demuth, DR [1 ]
机构
[1] UNIV PENN, SCH DENT MED, DEPT BIOCHEM, PHILADELPHIA, PA 19104 USA
关键词
D O I
10.1046/j.1365-2958.1997.2021577.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:183 / 190
页数:8
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