Abstract
Antigens detected by the complement-fixation (CF) test were prepared from [baby hamster kidney] BHK-21 cells infected with Pichinde virus. The preparations contained 2 antigens demonstrable by immunodiffusion. The antigen present in abundance was heat stable, Pronase resistant and had a MW of 20,000-30,000 as estimated by gel filtration. Polyacrylamide gel electrophoresis of purified antigen demonstrated two low-MW polypeptides. An identical antigenic determinant was found by disrupting purified virus with Nonidet P-40, but none of the viral polypeptides co-migrated with the polypeptides derived from purified CF antigen. Pronase digestion of disrupted virus did not alter antigenicity but degraded the viral peptides to sizes similar to those associated with the major CF antigen. The major CF antigen of Pichinde virus is a cleavage product of the structural proteins of the virus.