Abstract
Abstract Protein A, an Fc-reacting molecule from Staphylococcus aureus Cowan I, neutralized infectious vaccinia virus-IgG (Vac-IgG) and herpes simplex virus-IgG (HSV-IgG) complexes. The amount of protein A-mediated neutralization was dependent on the concentration of anti-viral IgG and protein A incubated with the virus. Upon attachment of protein A to the HSV-IgG complex a portion of the virus formed an infectious HSV-IgG-protein A complex which could be neutralized by anti-protein A serum. In addition, attachment of protein A to HSV-IgG was found to inhibit complement-mediated neutralization. Heat-extracted Jensen's protein A caused less neutralization of HSV-IgG than the enzyme-extracted protein A-1. The experiments indicate that molecular size may play a major role in the mechanism by which protein A as well as other immunoglobulin-reacting substances neutralize virus-IgG complexes.
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