JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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 Momose, F.
Right arrow Articles by Nagata, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Momose, F.
Right arrow Articles by Nagata, K.

Journal of Virology, February 2001, p. 1899-1908, Vol. 75, No. 4
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.4.1899-1908.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Cellular Splicing Factor RAF-2p48/NPI-5/BAT1/UAP56 Interacts with the Influenza Virus Nucleoprotein and Enhances Viral RNA Synthesis

Fumitaka Momose,1,dagger Christopher F. Basler,2 Robert E. O'Neill,2,Dagger Akihiro Iwamatsu,3 Peter Palese,2 and Kyosuke Nagata1,*

Laboratory of Molecular Medical Engineering, Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8501,1 and Central Laboratories for Key Technology, Kirin Brewery Company, Kanazawa-ku, Yokohama, Kanagawa 236-0004,3 Japan, and Department of Microbiology, Mount Sinai School of Medicine, New York, New York 10029-65742

Received 2 August 2000/Accepted 16 November 2000

Previous biochemical data identified a host cell fraction, designated RAF-2, which stimulated influenza virus RNA synthesis. A 48-kDa polypeptide (RAF-2p48), a cellular splicing factor belonging to the DEAD-box family of RNA-dependent ATPases previously designated BAT1 (also UAP56), has now been identified as essential for RAF-2 stimulatory activity. Additionally, RAF-2p48 was independently identified as an influenza virus nucleoprotein (NP)-interacting protein, NPI-5, in a yeast two-hybrid screen of a mammalian cDNA library. In vitro, RAF-2p48 interacted with free NP but not with NP bound to RNA, and the RAF-2p48-NP complex was dissociated following addition of free RNA. Furthermore, RAF-2p48 facilitated formation of the NP-RNA complexes that likely serve as templates for the viral RNA polymerase. RAF-2p48 was shown, in both in vitro binding assays and the yeast two-hybrid system, to bind to the amino-terminal region of NP, a domain essential for RNA binding. Together, these observations suggest that RAF-2p48 facilitates NP-RNA interaction, thus leading to enhanced influenza virus RNA synthesis.

* Corresponding author. Mailing address: Laboratory of Molecular Medical Engineering, Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan. Phone: 81 45-924-5798. Fax: 81 45-924-5804. E-mail: knagata{at}bio.titech.ac.jp.

dagger Present address: Department of Virology, Center for Basic Research, The Kitasato Institute, Minato-ku, Tokyo 108-8642, Japan.

Dagger Present address: Department of Viral Vaccine Research, Wyeth-Lederle Vaccines and Pediatrics, Pearl River, NY 10965.

Journal of Virology, February 2001, p. 1899-1908, Vol. 75, No. 4
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.4.1899-1908.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 2001 by the American Society for Microbiology. All rights reserved.