Heterogeneity of binding of human IgA subclasses to protein A.
The ability of human IgA myeloma immunoglobulins to interact with protein A-containing Staphylococcus aureus was examined. Some IgA1 and IgA2 immunoglobulins bound to S. aureus although others of both subclasses failed to do so. These results were obtained by using both direct binding of radiolabeled immunoglobulins to S. aureus and with inhibition-type assays. Binding was dependent on the Fc fragment of IgA since there was no binding to S. aureus by an F(ab')2 fragment of IgA1. Nonprotein A-containing bacteria did not bind these immunoglobulins and isolated protein A interacted with radiolabeled immunoglobulins. This strongly suggested that protein A was responsible for the observed binding to S. aureus. These data indicate, in contrast to previous reports, that there is no simple relationship between IgA subclass and the capacity to bind to protein A.
D001666:Binding Sites, Antibody; D006801:Humans; D007070:Immunoglobulin A / Q000276:immunology*; D007140:Immunoglobulin Fab Fragments / Q000276:immunology; D007075:Immunoglobulin M / Q000276:immunology; D007457:Iodine Radioisotopes; D008089:Listeria monocytogenes / Q000276:immunology; D009101:Multiple Myeloma / Q000276:immunology; D013205:Staphylococcal Protein A / Q000276:immunology*; D013211:Staphylococcus aureus / Q000276:immunology
D007070:Immunoglobulin A; D007140:Immunoglobulin Fab Fragments; D007075:Immunoglobulin M; D007457:Iodine Radioisotopes; D013205:Staphylococcal Protein A