This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tan, K. B. Articles by Sokol, F. Search for Related Content PubMed PubMed Citation Articles by Tan, K. B. Articles by Sokol, F.

Virion-Bound Protein Kinase in Semliki Forest and Sindbis Viruses

¹ The Wistar Institute of Anatomy and Biology, Philadelphia, Pennsylvania 19104

ABSTRACT

Semliki forest virus and Sindbis virus (Alphaviruses belonging to the togavirus group) grown in BHK-21 cells possessed very low levels of virion-associated protein kinase activity. For comparison, vesicular stomatitis virus, also grown in BHK-21 cells, contained a virion-bound protein kinase which had a specific activity 80 times greater than that of the Alphaviruses. The Alphavirus protein kinase was unmasked by the nonionic detergent Nonidet P-40 but was not activated by cyclic nucleotides. Phosvitin was the best exogenous phosphate acceptor for assaying the viral enzyme in vitro. Phosphoprotein phosphatase activity was also detected in the Alphaviruses. Both in vivo and in vitro, all of the viral structural polypeptides were phosphorylated, and the phosphorylated amino acids were found to be serine and threonine. The viral nucleocapsid protein was about four times more efficient as a phosphate acceptor than were the envelope proteins. From 33 to 50% of the total protein kinase was bound to the viral nucleocapsid, and the specific activity of this enzyme was 4 to 10 times greater than that associated with the viral envelope.

This article has been cited by other articles:

• Law, L. J., Ilkow, C. S., Tzeng, W.-P., Rawluk, M., Stuart, D. T., Frey, T. K., Hobman, T. C. (2006). Analyses of Phosphorylation Events in the Rubella Virus Capsid Protein: Role in Early Replication Events. J. Virol. 80: 6917-6925 [Abstract] [Full Text]