Antibody-mediated inhibition of dextran-sucrose-induced agglutination of Streptococcus mutans.
Immune sera to strains of Streptococcus mutans were found to inhibit agglutination of bacterial suspensions to which either high-molecular-weight dextran or sucrose was added. This inhibitory activity was shown to be mediated by antibody of the immunoglobulin G class. A semiquantitative assay was developed which demonstrated cross-inhibition of dextran/sucrose-induced agglutination among several strains of S. mutans. Antiserum to a partially purified glucosyltransferase was found to lack agglutination inhibition activity, consistent with the hypothesis that the dextran-binding antigen detected by the assay is immunologically distinct from the glucan-synthetic enzyme. A model for glucan synthesis and binding consistent with the reported data is described.
D000042:Absorption; D000371:Agglutination / Q000187:drug effects; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003429:Cross Reactions; D003911:Dextrans / Q000037:antagonists & inhibitors*; D005964:Glucosyltransferases / Q000378:metabolism; D007106:Immune Sera / Q000494:pharmacology*; D005779:Immunodiffusion; D008722:Methods; D011134:Polysaccharides / Q000096:biosynthesis; D013291:Streptococcus / Q000187:drug effects* / Q000378:metabolism; D013395:Sucrose / Q000037:antagonists & inhibitors*
D003911:Dextrans; D007106:Immune Sera; D011134:Polysaccharides; D013395:Sucrose; D005964:Glucosyltransferases