The role of soluble protein A in chicken spleen cell activation.
Soluble protein A (SpA) caused chicken spleen cell proliferation despite considerable evidence that SpA has no binding affinity for avian immunoglobulin (Ig). This biological activity was examined by several approaches. SpA-stimulated spleen cell cultures demonstrated no difference in proliferative responses regardless of the addition of human gamma globulin (HGG) or keyhole limpet hemocyanin. Adsorbents composed of HGG or hemoglobin were equally ineffective in abrogating the ability of SpA to induce spleen cell proliferation. In addition, ion exchange purified SpA was observed to induce comparable levels of spleen cell proliferation as ion exchange-affinity purified preparations. The lymphocyte subpopulation responsible for the observed proliferative response to SpA resides in the nylon wool adherent population. Nylon wool nonadherent lymphocytes failed to proliferate to SpA, but did proliferate in response to phytohemagglutinin as did nylon wool adherent cells. These data indicate that SpA is not responsible for the observed biological activity and suggest that components from Staphylococcus aureus other than SpA copurify during the preparation of SpA and are responsible for the activation of spleen cells.
D000818:Animals; D001402:B-Lymphocytes / Q000276:immunology; D002645:Chickens / Q000276:immunology*; D002845:Chromatography; D008213:Lymphocyte Activation; D012995:Solubility; D013154:Spleen / Q000276:immunology; D013205:Staphylococcal Protein A / Q000302:isolation & purification / Q000494:pharmacology*; D013601:T-Lymphocytes / Q000276:immunology; D005719:gamma-Globulins / Q000276:immunology
D013205:Staphylococcal Protein A; D005719:gamma-Globulins