DIFFERENTIATION OF SALIVARY AGGLUTININ-MEDIATED ADHERENCE AND AGGREGATION OF MUTANS STREPTOCOCCI BY USE OF MONOCLONAL-ANTIBODIES AGAINST THE MAJOR SURFACE ADHESIN-P1

被引:135
作者
BRADY, LJ
PIACENTINI, DA
CROWLEY, PJ
OYSTON, PCF
BLEIWEIS, AS
机构
关键词
D O I
10.1128/IAI.60.3.1008-1017.1992
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
The ability to adhere to salivary agglutinin-coated hydroxyapatite beads and to aggregate in the presence of fluid-phase salivary agglutinin was tested by using 25 isolates of mutans streptococci representing eight serotypes. Both adherence and aggregation activity correlated with expression of the M(r)-185,000 cell surface antigen P1 on Streptococcus mutans serotype c, e, and f strains. In addition, it was shown that the P1 molecule itself served as the adhesin of S. mutans serotype c, since adherence was significantly inhibited by the presence of recombinant-specified M(r)-150,000 P1. The ability of S. sobrinus strains to adhere or aggregate did not correlate with expression of the P1 cross-reactive antigen SpaA. There was also evidence for interaction with salivary agglutinin, as manifested by aggregation but not adherence of S. rattus serotype b, which does not express a P1 cross-reactive antigen. To understand the interaction of P1 with salivary agglutinin at the molecular level, a panel of 11 anti-P1 monoclonal antibodies was tested for inhibitory activity in adherence and aggregation inhibition assays. Overlapping, but not identical, subsets of monoclonal antibodies were found to inhibit adherence and aggregation, indicating that the interactions of P1 with salivary agglutinin which mediate these two phenomena are different. The localization of functional domains of P1 which may mediate the aggregation and adherence reactions is discussed.
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页码:1008 / 1017
页数:10
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