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 Eulálio, A.
Right arrow Articles by de Lima, M. C. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Eulálio, A.
Right arrow Articles by de Lima, M. C. P.

 Previous Article  |  Next Article 

Journal of Virology, February 2006, p. 1393-1404, Vol. 80, No. 3
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.3.1393-1404.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Nuclear Export of African Swine Fever Virus p37 Protein Occurs through Two Distinct Pathways and Is Mediated by Three Independent Signals

Ana Eulálio,1,2 Isabel Nunes-Correia,1,2 Ana Luísa Carvalho,1,3 Carlos Faro,1,2 Vitaly Citovsky,4 José Salas,5 Maria L. Salas,5 Sérgio Simões,1,6 and Maria C. Pedroso de Lima1,2*

Center for Neuroscience and Cell Biology of Coimbra, University of Coimbra, 3004-517 Coimbra, Portugal,1 Department of Biochemistry, Faculty of Sciences and Technology, University of Coimbra, 3001-401 Coimbra, Portugal,2 Department of Zoology, Faculty of Sciences and Technology, University of Coimbra, 3004-504 Coimbra, Portugal,3 Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, New York 11794-5215,4 Centro de Biología Molecular "Severo Ochoa" (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain,5 Department of Pharmaceutical Technology, Faculty of Pharmacy, University of Coimbra, 3000-295 Coimbra, Portugal6

Received 16 August 2005/ Accepted 16 November 2005

Nucleocytoplasmic shuttling activity of the African swine fever virus p37 protein, a major structural protein of this highly complex virus, has been recently reported. The systematic characterization of the nuclear export ability of this protein constituted the major purpose of the present study. We report that both the N- and C-terminal regions of p37 protein are actively exported from the nucleus to the cytoplasm of yeast and mammalian cells. Moreover, experiments using leptomycin B and small interfering RNAs targeting the CRM1 receptor have demonstrated that the export of p37 protein is mediated by both the CRM1-dependent and CRM1-independent nuclear export pathways. Two signals responsible for the CRM1-mediated nuclear export of p37 protein were identified at the N terminus of the protein, and an additional signal was identified at the C-terminal region, which mediates the CRM1-independent nuclear export. Interestingly, site-directed mutagenesis revealed that hydrophobic amino acids are critical to the function of these three nuclear export signals. Overall, our results demonstrate that two distinct pathways contribute to the strong nuclear export of full-length p37 protein, which is mediated by three independent nuclear export signals. The existence of overlapping nuclear export mechanisms, together with our observation that p37 protein is localized in the nucleus at early stages of infection and exclusively in the cytoplasm at later stages, suggests that the nuclear transport ability of this protein may be critical to the African swine fever virus replication cycle.

* Corresponding author. Mailing address: Department of Biochemistry, Faculty of Sciences and Technology, University of Coimbra, Apartado 3126, 3001-401 Coimbra, Portugal. Phone: 351239820190. Fax: 351239853607. E-mail: mdelima{at}ci.uc.pt.

Journal of Virology, February 2006, p. 1393-1404, Vol. 80, No. 3
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.3.1393-1404.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Reed, M. L., Howell, G., Harrison, S. M., Spencer, K.-A., Hiscox, J. A. (2007). Characterization of the Nuclear Export Signal in the Coronavirus Infectious Bronchitis Virus Nucleocapsid Protein. J. Virol. 81: 4298-4304 [Abstract] [Full Text]  
  • Epifano, C., Krijnse-Locker, J., Salas, M. L., Salas, J., Rodriguez, J. M. (2006). Generation of Filamentous Instead of Icosahedral Particles by Repression of African Swine Fever Virus Structural Protein pB438L. J. Virol. 80: 11456-11466 [Abstract] [Full Text]  
  • Verhagen, J., Donnelly, M., Elliott, G. (2006). Characterization of a Novel Transferable CRM-1-Independent Nuclear Export Signal in a Herpesvirus Tegument Protein That Shuttles between the Nucleus and Cytoplasm.. J. Virol. 80: 10021-10035 [Abstract] [Full Text]  
  • Lischka, P., Rauh, C., Mueller, R., Stamminger, T. (2006). Human Cytomegalovirus UL84 Protein Contains Two Nuclear Export Signals and Shuttles between the Nucleus and the Cytoplasm.. J. Virol. 80: 10274-10280 [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»