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 Bui, M.
Right arrow Articles by Whittaker, G. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bui, M.
Right arrow Articles by Whittaker, G. R.

 Previous Article  |  Next Article 

Journal of Virology, February 2000, p. 1781-1786, Vol. 74, No. 4
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Role of the Influenza Virus M1 Protein in Nuclear Export of Viral Ribonucleoproteins

Matthew Bui,1,dagger Elizabeth G. Wills,2 Ari Helenius,1,Dagger and Gary R. Whittaker2,*

Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510,1 and Department of Microbiology and Immunology, Cornell University, Ithaca, New York 148532

Received 28 July 1999/Accepted 18 November 1999

The protein kinase inhibitor H7 blocks influenza virus replication, inhibits production of the matrix protein (M1), and leads to a retention of the viral ribonucleoproteins (vRNPs) in the nucleus at late times of infection (K. Martin and A. Helenius, Cell 67:117-130, 1991). We show here that production of assembled vRNPs occurs normally in H7-treated cells, and we have used H7 as a biochemical tool to trap vRNPs in the nucleus. When H7 was removed from the cells, vRNP export was specifically induced in a CHO cell line stably expressing recombinant M1. Similarly, fusion of cells expressing recombinant M1 from a Semliki Forest virus vector allowed nuclear export of vRNPs. However, export was not rescued when H7 was present in the cells, implying an additional role for phosphorylation in this process. The viral NS2 protein was undetectable in these systems. We conclude that influenza virus M1 is required to induce vRNP nuclear export but that cellular phosphorylation is an additional factor.

* Corresponding author. Mailing address: C5141 Veterinary Medical Center, Cornell University, Ithaca, NY 14853. Phone: (607) 253-4019. Fax: (607) 253-3384. E-mail: grw7{at}cornell.edu.

dagger Present address: Department of Urology, UCLA Medical Center, Los Angeles, Calif.

Dagger Present address: Laboratorium für Biochemie, ETH-Zentrum, CH-8092 Zürich, Switzerland.

Journal of Virology, February 2000, p. 1781-1786, Vol. 74, No. 4
0022-538X/00/$04.00+0
Copyright © 2000, 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 © 2000 by the American Society for Microbiology. All rights reserved.