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

This Article Full Text 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 Google Scholar Google Scholar Articles by Schwemmle, M. Articles by Lipkin, W. I. Search for Related Content PubMed PubMed Citation Articles by Schwemmle, M. Articles by Lipkin, W. I. Social Bookmarking                      What's this?

Volume 272, Number 35, Issue of August 29, 1997 pp. 21818-21823
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Borna Disease Virus P-protein Is Phosphorylated by Protein Kinase C and Casein Kinase II

(Received for publication, December 24, 1996, and in revised form, May 20, 1997)

Martin Schwemmle , Bishnu De ^¶ , Licheng Shi , Amiya Banerjee ^¶ and W. Ian Lipkin

From the ^¶ Department of Molecular Biology, Research Institute, The Cleveland Clinic Foundation, Cleveland, Ohio 44195 and the  Laboratory for Neurovirology, Department of Neurology, Anatomy and Neurobiology, and Microbiology and Molecular Genetics, University of California, Irvine, California 92697-4290

Borna disease virus (BDV) is a newly classified nonsegmented negative-strand RNA virus (order of Mononegavirales) that persistently infects specific brain regions and circuits of warm-blooded animals to cause behavioral disturbances. Viruses within the order of Mononegavirales have phosphoproteins that typically serve as transcription factors and are modulated in functional activity through phosphorylation. To identify the kinases involved in BDV phosphoprotein (BDV-P) phosphorylation, in vitro phosphorylation assays were performed using recombinant phosphoprotein produced in Escherichia coli as substrate and cytoplasmic extracts from a rat glioma cell line (C6) or rat brain extracts as sources of kinase activity. These experiments revealed that BDV-P was phosphorylated predominantly by protein kinase C (PKC) and to a lesser extent by casein kinase II. Partial purification of the PKC from rat brain extract suggested that the BDV-P phosphorylating kinase is PKC. A role for PKC phosphorylation in vivo was confirmed by using the PKC-specific inhibitor GF109203X. Furthermore, peptide mapping studies indicated that BDV-P is phosphorylated at the same sites in vitro as it is in vivo. Mutational analysis identified Ser²⁶ and Ser²⁸ as sites for PKC phosphorylation and Ser⁷⁰ and Ser⁸⁶ as sites for casein kinase II phosphorylation. The anatomic distribution of PKC in the central nervous system may have implications for BDV neurotropism and pathogenesis.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				S. Schmid, D. Mayer, U. Schneider, and M. Schwemmle Functional Characterization of the Major and Minor Phosphorylation Sites of the P Protein of Borna Disease Virus J. Virol., June 1, 2007; 81(11): 5497 - 5507. [Abstract] [Full Text] [PDF]

				M. Schwardt, D. Mayer, R. Frank, U. Schneider, M. Eickmann, O. Planz, T. Wolff, and M. Schwemmle The negative regulator of Borna disease virus polymerase is a non-structural protein J. Gen. Virol., November 1, 2005; 86(11): 3163 - 3169. [Abstract] [Full Text] [PDF]

				G. Unterstab, S. Ludwig, A. Anton, O. Planz, B. Dauber, D. Krappmann, G. Heins, C. Ehrhardt, and T. Wolff Viral targeting of the interferon-{beta}-inducing Traf family member-associated NF-{kappa}B activator (TANK)-binding kinase-1 PNAS, September 20, 2005; 102(38): 13640 - 13645. [Abstract] [Full Text] [PDF]

				U. Schneider, M. Naegele, P. Staeheli, and M. Schwemmle Active Borna Disease Virus Polymerase Complex Requires a Distinct Nucleoprotein-to-Phosphoprotein Ratio but No Viral X Protein J. Virol., November 1, 2003; 77(21): 11781 - 11789. [Abstract] [Full Text] [PDF]

				T. Kobayashi, G. Zhang, B.-J. Lee, S. Baba, M. Yamashita, W. Kamitani, H. Yanai, K. Tomonaga, and K. Ikuta Modulation of Borna Disease Virus Phosphoprotein Nuclear Localization by the Viral Protein X Encoded in the Overlapping Open Reading Frame J. Virol., July 15, 2003; 77(14): 8099 - 8107. [Abstract] [Full Text] [PDF]

				F. MEGGIO and L. A. PINNA One-thousand-and-one substrates of protein kinase CK2? FASEB J, March 1, 2003; 17(3): 349 - 368. [Abstract] [Full Text] [PDF]

				O. Planz, S. Pleschka, and S. Ludwig MEK-Specific Inhibitor U0126 Blocks Spread of Borna Disease Virus in Cultured Cells J. Virol., May 15, 2001; 75(10): 4871 - 4877. [Abstract] [Full Text]

				M. P. Walker, I. Jordan, T. Briese, N. Fischer, and W. I. Lipkin Expression and Characterization of the Borna Disease Virus Polymerase J. Virol., May 1, 2000; 74(9): 4425 - 4428. [Abstract] [Full Text]

				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]

				M Schwemmle, C Jehle, T Shoemaker, and W. Lipkin Characterization of the major nuclear localization signal of the Borna disease virus phosphoprotein J. Gen. Virol., January 1, 1999; 80(1): 97 - 100. [Abstract]

				M. Schwemmle, M. Salvatore, L. Shi, J. Richt, C. H. Lee, and W. I. Lipkin Interactions of the Borna Disease Virus P, N, and X Proteins and Their Functional Implications J. Biol. Chem., April 10, 1998; 273(15): 9007 - 9012. [Abstract] [Full Text] [PDF]

				A. Hans, S. Syan, C. Crosio, P. Sassone-Corsi, M. Brahic, and D. Gonzalez-Dunia Borna Disease Virus Persistent Infection Activates Mitogen-activated Protein Kinase and Blocks Neuronal Differentiation of PC12 Cells J. Biol. Chem., March 2, 2001; 276(10): 7258 - 7265. [Abstract] [Full Text] [PDF]