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  • Title: Interaction of type II IgG Fc-receptors from streptococci of serological group A with murine IgG.
    Author: Lämmler C, Sting R.
    Journal: Zentralbl Bakteriol; 1989 Oct; 271(4):460-5. PubMed ID: 2684206.
    Abstract:
    A group A streptococcal strain demonstrated binding activities for 125I-murine IgG3 and 125I-human IgG. This 125I-murine IgG3 binding could be inhibited by unlabelled equine IgG but not by IgG from cattle, chickens and dogs, indicating binding properties of IgG Fc-receptors of type II. In contrast to binding sites of Streptococcus dysgalactiae (serogroup C) carrying type III IgG Fc-receptors, the binding sites of the group A streptococcus appeared to be antigenically different, extremely sensitive to trypsin and did not show any cross reactions with human albumin. The group A and group C streptococcal binding sites could be solubilized by lysozyme treatment of the bacteria and subsequently isolated by affinity chromatography on human IgG-Sepharose. Further analysis of the group A and group C streptococcal binding proteins by SDS-PAGE and Western blotting revealed numerous, almost identical protein bands with binding activities for 125I-murine IgG3.
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