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INTERACTION OF STREPTOCOCCI WITH THE Fc FRAGMENT OF IgG
Author(s) -
CHRISTENSEN POUL,
JOHANSSON BENGT G.,
KRONVALL GORAN
Publication year - 1976
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.1699-0463.1976.tb00001.x
Subject(s) - chemistry , myeloma protein , fragment crystallizable region , antibody , immunoglobulin g , microbiology and biotechnology , reactivity (psychology) , immunoglobulin fc fragments , group a , receptor , biology , immunology , biochemistry , medicine , alternative medicine , pathology
The capacity of human IgG to interact with β‐haemolytic streptococci was studied in order to localize the site of interaction on the IgG molecule. The reactivity of different proteolytic fragments of IgG with streptococci group A, type M 1 and type M 56, group C and group G, was investigated by measuring their inhibitory effect on the uptake of 125 I labelled IgG myeloma protein by the streptococci. Equivalent molar amounts of Fc fragment and undigested IgG inhibited the uptake of 125 I labelled IgG myeloma protein equally well while only slight inhibition was obtained by F(ab') 2 preparations. No reactivity was found with IgM, Fab orchymotrypsin produced fragment Fc', of IgG. The reactivity of IgG with the streptococci was localized to the Fc fragment. Since the Fc' fragment was non‐reactive, the CH2 domain was probably carrying the IgG structures involved in the interaction with streptococci.