Identification and analysis of vaccinia virus palmitylproteins

Vaccinia virus encodes at least eight proteins that incorporate label from tritiated palmitic acid when it is added to infected cell cultures. Three o f these palmitylproteins are encoded by the A33R, B5R, and F13L open readin g 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 wit h 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 comp osed of the B5R protein and possibly others. All vaccinia-encoded palmitylp roteins are present in the membranous fraction of cells and are specific fo r the trans-Golgi network membrane-enveloped forms of the virus, suggesting that these proteins play a role in the envelopment and egress of virions o r the infectivity of released virus. (C) 2000 Academic Press.