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Binding of human IgA to HCl‐extracted c protein from group B streptococci (GBS)
Author(s) -
KVAM AUGUSTA IRENE,
IVERSEN OLEJAN,
BEVANGER LARS
Publication year - 1992
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1699-0463.1992.tb04050.x
Subject(s) - conjugate , antigen , immunofluorescence , group a , antibody , blot , receptor , group b , microbiology and biotechnology , biology , chemistry , biochemistry , immunology , medicine , mathematical analysis , mathematics , gene
The cβ protein of group B streptococci obtained by HCl extraction appears as a ladder‐like pattern in SDS‐PAGE when detected by a rabbit anti‐cβ serum, and a similar picture is seen when the crude extract is incubated with human IgA and an anti‐human IgA conjugate. Affinity‐purified cβ antigen and IgA receptors from GBS gave identical pictures in Western blots using rabbit anti‐cβ serum. Both the cβ antigen and the IgA receptor are exposed on the surface of GBS as demonstrated by immunofluorescence.