Multiple anti-cytokine activities secreted from tanapox virus-infected cells.

Tanapox virus (TPV) produces a mild disease in humans characterized by transient fever, one or more nodular skin lesions and regional lymphadenopathy. We demonstrate that TPV-infected cells, but not mock-infected cells, secrete an early 38 kDa glycopeptide that, unlike any other known protein, binds to human (h) interferon-gamma, hIL-2 and hIL-5. In concomitant experiments this polypeptide failed to bind to hIL-1 alpha, hIL-3, hIL-4, hIL-6, hIL-7, hIL-8 or hIL-10. Inhibition of hIL-2 and hIL-5 biological activities were demonstrated using a hIL-2-dependent mouse T cell line (HT-2) and a hIL-5-dependent erythroleukemia cell line (TF-1), respectively. The 38 kDa polypeptide also inhibited the bioactivity of interferon-gamma. Taken together, our results suggest that TPV has evolved multiple pathways to disarm both TH1 cell-mediated (IL-2 and interferon-gamma) and TH2-associated (IL-5) immune responses for its infectivity with remarkable genetic economy.