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THE GROUP A STREPTOCOCCAL RECEPTOR FOR HUMAN IgA BINDS IgA VIA THE Fc‐FRAGMENT
Author(s) -
SCHALÉN CLAËS
Publication year - 1980
Publication title -
acta pathologica microbiologica scandinavica section c immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0304-1328
DOI - 10.1111/j.1699-0463.1980.tb00105.x
Subject(s) - myeloma protein , polyclonal antibodies , immunoglobulin a , microbiology and biotechnology , antibody , chemistry , strain (injury) , protease , receptor , biology , immunoglobulin g , biochemistry , immunology , enzyme , anatomy
Eight freshly isolated type M4 strains of group A streptococci were found to bind between 60 and 80% of 2.5 μg radiolabelled IgA myeloma protein in a standard test system, while a reference type 4 strain bound only 20%. Commercial human IgG or IgGl myeloma protein did not inhibit the binding of IgA by the reference type 4 strain or one of the freshly isolated type 4 strains, whereas inhibition was obtained by purified polyclonal IgA and IgA I myeloma protein. Fc fragments of purified IgA I myeloma protein, obtained by digestion with gonococcal protease, inhibited binding of radiolabelled IgA I, while the Fab fragments had no inhibitory effect.