Antigenic diversity of IgA receptors in Streptococcus pyogenes.
In a previous study, group A and group B streptococcal IgA receptors were shown to differ serologically, in agreement with their known structural unrelatedness. The present study was undertaken to serologically compare the IgA binding epitopes of group A streptococcal strains representing various serotypes by the use of antisera to this species. It was found that blocking antibodies occurred in antisera to IgA binding but not to non-binding strains and that binding of IgA to a streptococcal strain was generally blocked by antiserum to the homologous type. However, cross-testing of a panel of 11 IgA binding strains, representing various M and T serotypes, with 10 different antisera to group A streptococci, demonstrated that IgA receptors were inhibited to a highly variable degree and that inhibition patterns were unique for each type. Comparing solubilized IgA receptors of various strains in immunoblot experiments, a variation in the molecular mass, between approximately 35 and 45 kDa, emerged. The IgA binding epitopes, analogous to protective sites of streptococcal M-protein, thus exhibited hypervariability which may suggest that IgA binding also plays a key role for evading host immune defence mechanisms.
Burova
L A
LA
Institute of Experimental Medicine, Academy of the Medical Sciences, St. Petersburg, Russia.
Schalén
C
C
D000818:Animals; D007106:Immune Sera / Q000276:immunology; D007070:Immunoglobulin A / Q000378:metabolism*; D008970:Molecular Weight; D011817:Rabbits; D011961:Receptors, Fc; D011971:Receptors, Immunologic / Q000032:analysis / Q000276:immunology*; D013297:Streptococcus pyogenes / Q000276:immunology*
C045281:IgA receptor; D007106:Immune Sera; D007070:Immunoglobulin A; D011961:Receptors, Fc; D011971:Receptors, Immunologic