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. 1973 Jun;11(6):961–970. doi: 10.1128/jvi.11.6.961-970.1973

Phosphoprotein Component of Vaccinia Virions

Hortencia Rosemond 1, Bernard Moss 1
PMCID: PMC355204  PMID: 4712965

Abstract

The recent discovery of a protein kinase activity in vaccinia virions led us to search for a viral protein which is phosphorylated in vivo. Vaccinia virus was radioactively labeled by infecting cells in the presence of 32P1. A phosphoprotein was isolated from purified delipidated virions by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The phosphoprotein appeared to be a specific viral component induced after infection. More than 60% of the phosphoprotein was associated with viral cores. The electrophoretic mobility of the protein suggested that it has a molecular weight of 11,000 to 12,000. Phosphoserine was liberated by acid hydrolysis and identified by electrophoresis with known standards. Tryptic digests of the purified phosphoprotein were analyzed by two-dimensional electrophoresis and chromatography on thin-layer cellulose plates, and a single major phosphopeptide was resolved. The high selectivity of phosphorylation suggested that the process has a specific function.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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