Capsid Components of the Parvovirus H-1 1

Abstract

Summary

Disruption of purified H-1 virions with sodium dodecyl sulfate (SDS) and mercaptoethanol (ME) at 100° and pH 7.2 results in the appearance of one major and two minor migrating components on polyacrylamide gels. Molecular weights of 92, 000 (A), 72,000 (B), and 56,000 (C) were determined for the three moieties by coelectrophoresis of the dissociated virus with reference proteins of known molecular weight. Electrophoretic separation of ¹⁴C- or ³H-labeled virus polypeptides showed the relative amount of each radioactive component to be 15% (A), 75% (B) and 10% (C) of the total viral protein. Elution of the components from the gels, followed by hemagglutination assay against guinea pig red blood cells, indicated that component B was the antigenic component and structural protein. Amino acid analyses of H-1 virions revealed an overall acidic nature of the protein (acidic/basic amino acids = 1.75).

The authors thank Miss Barbara Madden for technical assistance and Mr. Chad Shepis, University of Vermont, for performing the amino acid analyses.