Virus-specific basic phosphoproteins associated with herpes simplex virus type a (HSV-1) particles and the chromatin of HSV-1-infected cells.
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.
D000818:Animals; D002460:Cell Line; D002522:Chlorocebus aethiops; D002843:Chromatin / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel / Q000295:instrumentation; D000882:Haplorhini; D006851:Hydrochloric Acid; D007668:Kidney; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D010750:Phosphoproteins / Q000032:analysis*; D018139:Simplexvirus / Q000032:analysis*; D012995:Solubility; D014764:Viral Proteins / Q000032:analysis*
D002843:Chromatin; D010455:Peptides; D010750:Phosphoproteins; D014764:Viral Proteins; D006851:Hydrochloric Acid