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Binding of immunoglobulin G and albumin to Streptococcus dysgalactiae
All 24 cultures of Streptococcus dysgalactiae investigated bound 125I-IgG, 13 cultures additionally interacted with 125I-albumin. Inhibition experiments with unlabelled IgG and albumin preparations from humans and various animal species indicated the specificity of the binding sites which showed characteristics of IgG Fc-receptors of type III and albumin-receptors of type c. IgG and albumin-binding proteins could be removed from the streptococcal surface by solubilization and subsequently isolated by affinity chromatography. The isolated binding proteins of S. dysgalactiae strains C 12 and C 8 obtained from IgG and albumin sepharose precipitated with IgG in immunodiffusion reactions, and in immunoelectrophoretic studies, and they reacted, after transfer onto nitrocellulose, with 125I-IgG or 125I-albumin and vice versa. Antisera produced against IgG-binding proteins of S. dysgalactiae C 12 inhibited binding of 125I-IgG and 125I-albumin. Solubilization of binding proteins by trypsinization yielded low molecular weight fragments with 125I-IgG but not with 125I-albumin binding activities. IgG-binding proteins isolated from S. dysgalactiae C 26 reacted with 125I-IgG but not with 125I-albumin, indicating the presence of 2 groups of type III Fc-receptors among S. dysgalactiae strains.
All 24 cultures of Streptococcus dysgalactiae investigated bound 125I-IgG, 13 cultures additionally interacted with 125I-albumin. Inhibition experiments with unlabelled IgG and albumin preparations from humans and various animal species indicated the specificity of the binding sites which showed characteristics of IgG Fc-receptors of type III and albumin-receptors of type c. IgG and albumin-binding proteins could be removed from the streptococcal surface by solubilization and subsequently isolated by affinity chromatography. The isolated binding proteins of S. dysgalactiae strains C 12 and C 8 obtained from IgG and albumin sepharose precipitated with IgG in immunodiffusion reactions, and in immunoelectrophoretic studies, and they reacted, after transfer onto nitrocellulose, with 125I-IgG or 125I-albumin and vice versa. Antisera produced against IgG-binding proteins of S. dysgalactiae C 12 inhibited binding of 125I-IgG and 125I-albumin. Solubilization of binding proteins by trypsinization yielded low molecular weight fragments with 125I-IgG but not with 125I-albumin binding activities. IgG-binding proteins isolated from S. dysgalactiae C 26 reacted with 125I-IgG but not with 125I-albumin, indicating the presence of 2 groups of type III Fc-receptors among S. dysgalactiae strains.