Identification and analysis of vaccinia virus palmitylproteins

D. W. Grosenbach, S. G. Hansen, D. E. Hruby

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

Vaccinia virus encodes at least eight proteins that incorporate label from tritiated palmitic acid when it is added to infected cell cultures. Three of these palmitylproteins are encoded by the A33R, B5R, and F13L open reading frames and migrate by gel electrophoresis with relative molecular masses of 23-28, 42, and 37 kDa, respectively. In this report we provide evidence that the A22R and A36R open reading frames also encode palmitylproteins with apparent molecular masses of 22 and 50-55 kDa, respectively. Furthermore, the hemagglutinin protein (A56R) from the Copenhagen strain is shown to be palmitylated while the hemagglutinin protein from the WR and IHD-J strains is not. A 94-kDa VV palmitylprotein appears to be a multimeric complex composed of the B5R protein and possibly others. All vaccinia-encoded palmitylproteins are present in the membranous fraction of cells and are specific for the trans-Golgi network membrane-enveloped forms of the virus, suggesting that these proteins play a role in the envelopment and egress of virions or the infectivity of released virus. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)193-206
Number of pages14
JournalVirology
Volume275
Issue number1
DOIs
StatePublished - Sep 15 2000

ASJC Scopus subject areas

  • Virology

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