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
Google Scholar
Right arrow Articles by Schneider, J.
Right arrow Articles by Wolff, T.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schneider, J.
Right arrow Articles by Wolff, T.

 Previous Article  |  Next Article 

Journal of Virology, January 2009, p. 701-711, Vol. 83, No. 2
0022-538X/09/$08.00+0     doi:10.1128/JVI.01858-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Analysis of Influenza B Virus NS1 Protein Trafficking Reveals a Novel Interaction with Nuclear Speckle Domains{triangledown}

Jana Schneider,1 Bianca Dauber,1,{dagger} Krister Melén,2 Ilkka Julkunen,2 and Thorsten Wolff1*

Robert Koch-Institute, Nordufer 20, 13353 Berlin, Germany,1 Departments of Viral Diseases and Immunology, National Public Health Institute, FIN-00300, Helsinki, Finland2

Received 3 September 2008/ Accepted 27 October 2008

Many proteins that function in the transcription, maturation, and export of metazoan mRNAs are concentrated in nuclear speckle domains, indicating that the compartment is important for gene expression. Here, we show that the NS1 protein of influenza B virus (B/NS1) accumulates in nuclear speckles and causes rounding and morphological changes of the domains, indicating a disturbance in their normal functions. This property was located within the N-terminal 90 amino acids of the B/NS1 protein and was shown to be independent of any other viral gene product. Within this protein domain, we identified a monopartite importin {alpha} binding nuclear localization signal. Reverse-genetic analysis of this motif indicated that nuclear import and speckle association of the B/NS1 protein are required for the full replication capacity of the virus. In the late phase of virus infection, the B/NS1 protein relocated to the cytoplasm, which occurred in a CRM1-independent manner. The interaction of the B/NS1 protein with nuclear speckles may reflect a recruitment function to promote viral-gene expression. To our knowledge, this is the first functional description of a speckle-associated protein that is encoded by a negative-strand RNA virus.

* Corresponding author. Mailing address: Robert Koch-Institute, P15, Nordufer 20, 13353 Berlin, Germany. Phone: 49-30-187542278. Fax: 49-30-187542328. E-mail: WolffT{at}RKI.de

{triangledown} Published ahead of print on 5 November 2008.

{dagger} Present address: Alberta Institute for Viral Immunology, Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Canada.

Journal of Virology, January 2009, p. 701-711, Vol. 83, No. 2
0022-538X/09/$08.00+0     doi:10.1128/JVI.01858-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Han, Z., Alves, C., Gudima, S., Taylor, J. (2009). Intracellular Localization of Hepatitis Delta Virus Proteins in the Presence and Absence of Viral RNA Accumulation. J. Virol. 83: 6457-6463 [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»