Abstract
Herpes simplex type 1 Angelotti (HSV-1 ANG) virions contain 2 major acid-soluble proteins, BP1 and 2, which by size and charge analysis were also associated with chromatin isolated from HSV-1 ANG-infected African green monkey kidney cells (HSV-chromatin). BP1 and 2 existed in a phosphorylated state in virions and in HSV-chromatin. BP1 consisted of a single polypeptide of 38 K [kilodaltons] MW which was correlated to the tegument protein VP22. In SDS[sodium dodecyl sulfate]-polyacrylamide gels BP2 migrated as a single polypeptide band with an apparent MW of 12 K. Urea gel analysis revealed that BP2 consisted of 3 components, BP2a, b and c, of different phosphate contents. These components probably represent different polypeptides of similar MW. HSV-chromatin, BP1, BP2a, b and c contained a further major virus-induced basic phosphopolypeptide of MW 65 K which was not detected in acid-extracts of mature virions.