This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chase, G.
Right arrow Articles by Schwemmle, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chase, G.
Right arrow Articles by Schwemmle, M.

 Previous Article  |  Next Article 

Journal of Virology, January 2007, p. 743-749, Vol. 81, No. 2
0022-538X/07/$08.00+0     doi:10.1128/JVI.01351-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Borna Disease Virus Matrix Protein Is an Integral Component of the Viral Ribonucleoprotein Complex That Does Not Interfere with Polymerase Activity{triangledown}

Geoffrey Chase,1 Daniel Mayer,1 Antonia Hildebrand,1 Ronald Frank,2 Yohei Hayashi,3 Keizo Tomonaga,3 and Martin Schwemmle1*

Department of Virology, Institute for Medical Microbiology and Hygiene, University of Freiburg, Freiburg,1 Department of Chemical Biology, Helmholtz Center for Infection Research, Braunschweig, Germany,2 Department of Virology, Research Institute for Microbial Diseases (BIKEN), Osaka University, Osaka, Japan3

Received 27 June 2006/ Accepted 22 October 2006

We have recently shown that the matrix protein M of Borna disease virus (BDV) copurifies with the affinity-purified nucleoprotein (N) from BDV-infected cells, suggesting that M is an integral component of the viral ribonucleoprotein complex (RNP). However, further studies were hampered by the lack of appropriate tools. Here we generated an M-specific rabbit polyclonal antiserum to investigate the intracellular distribution of M as well as its colocalization with other viral proteins in BDV-infected cells. Immunofluorescence analysis revealed that M is located both in the cytoplasm and in nuclear punctate structures typical for BDV infection. Colocalization studies indicated an association of M with nucleocapsid proteins in these nuclear punctate structures. In situ hybridization analysis revealed that M also colocalizes with the viral genome, implying that M associates directly with viral RNPs. Biochemical studies demonstrated that M binds specifically to the phosphoprotein P but not to N. Binding of M to P involves the N terminus of P and is independent of the ability of P to oligomerize. Surprisingly, despite P-M complex formation, BDV polymerase activity was not inhibited but rather slightly elevated by M, as revealed in a minireplicon assay. Thus, unlike M proteins of other negative-strand RNA viruses, BDV-M seems to be an integral component of the RNPs without interfering with the viral polymerase activity. We propose that this unique feature of BDV-M is a prerequisite for the establishment of BDV persistence.

* Corresponding author. Mailing address: Department of Virology, University of Freiburg, Hermann-Herder-Strasse 11, D-79104 Freiburg, Germany. Phone: 49-761-203-6526. Fax: 49-761-203-6639. E-mail: martin.schwemmle{at}uniklinik-freiburg.de.

{triangledown} Published ahead of print on 1 November 2006.

Journal of Virology, January 2007, p. 743-749, Vol. 81, No. 2
0022-538X/07/$08.00+0     doi:10.1128/JVI.01351-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Neumann, P., Lieber, D., Meyer, S., Dautel, P., Kerth, A., Kraus, I., Garten, W., Stubbs, M. T. (2009). Crystal structure of the Borna disease virus matrix protein (BDV-M) reveals ssRNA binding properties. Proc. Natl. Acad. Sci. USA 106: 3710-3715 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»