Herpes simplex type 1 Angelotti (HSV-1 ANG) virions were shown to contain two major acid-soluble proteins, BP1 and 2, which by size and charge analysis were also found to be associated with chromatin isolated from HSV-1 ANG-infected African green monkey kidney cells (HSV-chromatin). BP1 and 2 proved to exist in a phosphorylated state both in virions and in HSV-chromatin. BP1 consisted of a single polypeptide of 38 K mol. wt. which was correlated to the tegument protein VP22. In SDS-polyacrylamide gels BP2 migrated as a single polypeptide band with an apparent mol. wt. of 12 K. Urea gel analysis revealed that BP2 consisted of three components, BP2a, b and c, of different phosphate contents. Arguments were provided that these components probably represent different polypeptides of similar mol. wt. HSV-chromatin, in addition to BP1, BP2a, b and c contained a further major virus-induced basic phosphopolypeptide of mol. wt. 65 K which was not detected in acid-extracts of mature virions.


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