Human peripheral blood lymphocyte activation by protein A from Staphylococcus aureus.
Mitogenesis and polyclonal immunoglobulin production in peripheral blood lymphocyte cultures activated with Formalin-fixed or autoclaved protein A-containing Staphylococcus aureus were studied. Direct evidence for a dissociation between cell proliferation and polyclonal immunoglobulin production was found, in that S. aureus was not mitogenic after being autoclaved but retained the ability to stimulate B cells to produce immunoglobulin. Trypsin-treated S. aureus lost its binding site for immunoglobulin G, but its mitogenicity was not altered; thus, the protein A binding site for immunoglobulin G on the bacterial cell wall is not required for the stimulation of lymphocyte proliferation. Our data also show a dissociation between cell proliferation and polyclonal immunoglobulin production induced by protein A coupled to Sepharose CL-4B. These results suggest the presence of three distinct active sites on the protein A molecule: one that binds immunoglobulin G molecules, one that stimulates cell proliferation, and one that stimulates polyclonal immunoglobulin production.
D001402:B-Lymphocytes / Q000276:immunology*; D002455:Cell Division; D006358:Hot Temperature; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D008213:Lymphocyte Activation; D008934:Mitogens / Q000494:pharmacology; D013205:Staphylococcal Protein A / Q000378:metabolism / Q000494:pharmacology*; D013211:Staphylococcus aureus / Q000276:immunology*; D014357:Trypsin / Q000494:pharmacology
D007074:Immunoglobulin G; D008934:Mitogens; D013205:Staphylococcal Protein A; D014357:Trypsin