Characterization of polypeptides immunoprecipitable from Pichinde virus-infected BHK-21 cells

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Abstract
Using hamster anti-Pichinde virus serum polypeptides were immunoprecipitated from BHK-21 (hamster kidney) cells infected with Pichinde virus. Seven immunoprecipitable polypeptides exhibted a time- and multiplicity of infection-dependent appearance when the cultures were pulse-labeled with L-[35S]methionine for 1 h. The predominant polypeptide was a nucleoprotein (NP) of 64,000 daltons. Components of 48,000, 38,000 and 28,000 daltons, when analyzed by 2-dimensional tryptic peptide mapping, were found to be derived from NP. After a 3-h chase, polypeptides of 17,000, 16,500 and 14,000 daltons were evident and peptide mapping revealed that these 3 polypeptides were also related to NP. During a series of pulse-chase experiments, a 79,000-dalton glycoprotein (GPC) was cleaved to glycoproteins of 52,000 and 36,000 daltons. Radiolabel in a polypeptide of approximately 200,000 daltons (L) did not chase into smaller cleavage products. L, GPC and NP were found to be unique by 2-dimensional tryptic peptide mapping. Comparison of polypeptides immunoprecipitated from infected cells with structural components of purified virus revealed that L protein was evident in both. This is the 1st report of a high MW polypeptide in Pichinde virus particles and infected cells.