Binding of murine myeloma proteins of different Ig classes and subclasses to Fc-reactive surface structures in gram-positive cocci.

Twelve different murine myeloma proteins were tested for binding to seventy Gram-positive strains belonging to group A, C and G streptococci and to Staphylococcus aureus. Group A streptococci, known to bind human IgG, were incapable of binding any of eight murine IgG immunoglobulins tested except for one strain that bound an IgG2b myeloma protein. In contrast, group C and G streptococci interacted with murine immunoglobulins of subclasses IgG2a, IgG2b and IgG3, and G strains also to a lesser extent with IgG1. Bovine and equine-group C streptococci did not differ from human group C streptococci in their IgG reactivity. Staphylococcal strains showed a high reactivity with murine myeloma components of IgG subclasses 2a, 2b and 3 and a low but definite binding of an IgG1 myeloma protein. IgA myeloma protein S-122 interacted with nine of fifteen group A streptococci. This binding could not be inhibited by human IgG and the reactivity is thus different from Fc-mediated binding of immunoglobulins. One of three IgA myeloma proteins tested, TEPC 15, bound to staphylococci. The Fc specificity of this interaction was confirmed by chromatography on protein A-Sepharose and by inhibition studies using polyclonal human IgG. The protein A reactivity of this monoclonal protein was detected in IgA aggregates and absent in the monomeric form of IgA.