HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Tuffereau, C. Articles by Flamand, A. Search for Related Content PubMed PubMed Citation Articles by Tuffereau, C. Articles by Flamand, A. Agricola Articles by Tuffereau, C. Articles by Flamand, A.

Phosphorylation of the N and M₁ Proteins of Rabies Virus

Laboratorie de Génétique des Virus, CNRS, 91190 Gif sur Yvette
and¹ Unité 15 INSERM, 24 rue du Faubourg St Jacques, 75014 Paris, France

Phosphorylation of rabies virus proteins was followed in vivo and in vitro. The N and M₁ proteins were both found to be phosphorylated. The M₁ protein was present in the virion in two phosphorylated states, but only the hypophosphorylated form of M₁ was found in infected cells. The hypothesis that some of the M₁ molecules become hyperphosphorylated during the maturation process by a membrane-bound kinase was examined. The phosphorylation of the viral proteins by the kinase present in purified rabies virions was studied using an in vitro transcriptase assay: under the conditions of the assay, additional phosphate groups were rapidly attached to the N protein. The M₁ protein was similarly hyperphosphorylated although more slowly. Whether the hyperphosphorylation of the N protein is responsible for the poor efficiency of the in vitro transcriptase reaction is not clear. No detectable change in the phosphorylation of cellular proteins was observed in the course of rabies virus infection.

Keywords: rabies virus, phosphorylation, kinase activity

Received 4 June 1985; accepted 5 July 1985.

This article has been cited by other articles:

				J.-J. Mu, D.-S. Chen, and P.-J. Chen The Conserved Serine 177 in the Delta Antigen of Hepatitis Delta Virus Is One Putative Phosphorylation Site and Is Required for Efficient Viral RNA Replication J. Virol., October 1, 2001; 75(19): 9087 - 9095. [Abstract] [Full Text] [PDF]

				A. K. Gupta, D. Blondel, S. Choudhary, and A. K. Banerjee The Phosphoprotein of Rabies Virus Is Phosphorylated by a Unique Cellular Protein Kinase and Specific Isomers of Protein Kinase C J. Virol., January 1, 2000; 74(1): 91 - 98. [Abstract] [Full Text]

				K. Kaelin, S. Dezélée, M. J. Masse, F. Bras, and A. Flamand The UL25 Protein of Pseudorabies Virus Associates with Capsids and Localizes to the Nucleus and to Microtubules J. Virol., January 1, 2000; 74(1): 474 - 482. [Abstract] [Full Text]

				M. Chenik, M. Schnell, K. K. Conzelmann, and D. Blondel Mapping the Interacting Domains between the Rabies Virus Polymerase and Phosphoprotein J. Virol., March 1, 1998; 72(3): 1925 - 1930. [Abstract] [Full Text] [PDF]

				D. B. Fishbein and L. E. Robinson Rabies N. Engl. J. Med., November 25, 1993; 329(22): 1632 - 1638. [Full Text]