Characterization of the mRNA's for the polyoma virus capsid proteins VP1, VP2, and VP3

T. Hunter, W. Gibson

Research output: Contribution to journalArticle

Abstract

Polyadenylated cytoplasmic RNA from polyoma virus-infected cells can be translated in the wheat germ system to yield all three polyoma virus capsid proteins, VP1, VP2, and VP3. The translation products of RNA selected from total cytoplasmic RNA of infected cells by hybridization to polyoma virus DNA showed a high degree of enrichment for VP1, VP2, and VP3. The identity of the in vitro products with authentic viron proteins was established in two ways. First, tryptic peptide maps of the in vitro products were found to be essentially identical to those of their in vivo counterparts. Second, the mobilities of the in vitro products on two-dimensional gels were the same as those of viral proteins labeled in vivo. VP1, VP2, and VP3 were all labeled with [35S]formylmethionine when they were synthesized in the presence of [35S]formylmethionyl-tRNA(f)(met). We determined the sizes of the polyadenylated mRNA's for VP1, VP2, and VP3 by fractionation on gels. The sizes of the major mRNA species for the capsid proteins are as follows: VP2, 8.5 x 105 daltons; VP3, 7.4 x 105 daltons; and VP1, 4.6 x 105 daltons. We conclude that all three viral capsid proteins are synthesized independently in vitro, that all three viral capsid proteins are virally coded, and that each of the capsid proteins has a discrete mRNA.

Original languageEnglish (US)
Pages (from-to)240-253
Number of pages14
JournalJournal of virology
Volume28
Issue number1
StatePublished - Dec 1 1978
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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