Proteins specified by herpesvirus saimiri: Identification and properties of virus-specific polypeptides in productively infected cells

R. E. Randall, R. W. Honess, P. O'Hare

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14 Citations (Scopus)

Abstract

The synthesis and accumulation of more than 30 virus-induced polypeptides was detected after infection of permissive primate cells with high multiplicities of herpesvirus saimiri. These virus-induced polypeptides had apparent mol. wt. of from 12000 (12 K) to 250 K and differed in molar abundance by up to two orders of magnitude. The majority of virus-induced polypeptides satisfied multiple criteria for their virus specificity. Polypeptides of 110 K, 76 K, 51 K and 31 K to 29 K were synthesized at maximum rates early in infection, but the majority of proteins were made at high rates late in infection. Virus-specific polypeptides were substrates for a number of post-synthetic modifications. The 117 K, 85 K, 76 K, 31 K and 30 K polypeptides were each processed to forms with altered electrophoretic mobility. The 117 K and 85 K polypeptides were among the virus-specified substrates for glycosylation and virus-induced polypeptides of 59 K, 51 K, 30 K and 26 K were phosphorylated. The early 51 K phosphoprotein and the 30 K to 31 K polypeptides were rapidly translocated to the nucleus of infected cells. The 31 K polypeptide was processed to a 29 K product which remained stably associated with the nuclear fraction. The 30 K nuclear protein was shown to be the precursor of a 28 K polypeptide which was released in a soluble form into the cytoplasmic fraction and the culture medium of cells at late times in the virus growth cycle. Many other polypeptides accumulated slowly in nuclear (e.g. 250 K, 150 K, 130 K, 110 K and 38 K) or in cytoplasmic (e.g. 117 K, 85 K and 28 K) fractions of infected cells in forms which could be differentiated by the use of detergents or differences in stability to salt extraction. The mol. wt., relative molarities and some features of the post-synthetic processing of herpesvirus saimiri polypeptides more closely resembled the properties of gene products of Epstein-Barr virus than those of herpes simplex virus.

Original languageEnglish
Pages (from-to)19-35
Number of pages17
JournalJournal of General Virology
Volume64
Issue number1
DOIs
Publication statusPublished - 1 Jan 1983

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