Identification of two functional forms of immunoglobulin G3-binding protein expressed by group A streptococci.

Analysis of group A streptococcal immunoglobulin G (IgG)-binding protein reactivity with different human IgG3-myeloma proteins provided evidence for at least two functional forms of these molecules. Representative IgG3-binding molecules were isolated, biotinylated, and used as tracers in competitive binding assays. Cross-inhibition studies demonstrated the existence of two distinct patterns of IgG3-binding activity. Proteins of one form could be inhibited from binding to an IgG3-myeloma protein by streptococcal protein G while binding of the second form was not inhibited. These studies further underscore the extent of heterogeneity among immunoglobulin-binding proteins expressed by group A streptococci.