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Journal of Virology, March 2004, p. 2979-2983, Vol. 78, No. 6
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.6.2979-2983.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Cells Expressing the RING Finger Z Protein Are Resistant to Arenavirus Infection

Tatjana I. Cornu,1 Heinz Feldmann,2 and Juan Carlos de la Torre1*

Division of Virology, Department of Neuropharmacology, The Scripps Research Institute, La Jolla, California 92037,1 Special Pathogens Program, National Microbiology Laboratory, Health Canada, Winnipeg, Manitoba, Canada R3E 3R22

Received 12 September 2003/ Accepted 18 November 2003

Arenaviruses include Lassa fever virus (LFV) and the South American hemorrhagic fever viruses. These viruses cause severe human disease, and they pose a threat as agents of bioterrorism. Arenaviruses are enveloped viruses with a bisegmented negative-strand RNA genome whose proteomic capability is limited to four polypeptides: nucleoprotein (NP); surface glycoprotein (GP), which is proteolytically processed into GP1 and GP2; polymerase (L); and a small (11-kDa) RING finger protein (Z). Our investigators have previously shown that Z has a strong inhibitory activity on RNA synthesis mediated by the polymerase of the prototypic arenavirus, lymphocytic choriomeningitis virus (LCMV). In this report we show that cells transduced with a replication-deficient recombinant adenovirus expressing Z (rAd-Z) are resistant to LCMV and LFV infection. Virus cell entry mediated by LCMV or LFV GP was not affected in rAd-Z-transduced cells, but both virus transcription and replication were strongly and specifically inhibited, which resulted in a dramatic reduction in production of infectious virus. These findings open new avenues for developing antiviral strategies to combat the highly pathogenic human arenaviruses, including LFV.

* Corresponding author. Mailing address: Dept. of Neuropharmacology, The Scripps Research Institute, IMM-6, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Phone: (858) 784-9462. Fax: (858) 784-9981. E-mail: juanct{at}scripps.edu.

Journal of Virology, March 2004, p. 2979-2983, Vol. 78, No. 6
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.6.2979-2983.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Casabona, J. C., Levingston Macleod, J. M., Loureiro, M. E., Gomez, G. A., Lopez, N. (2009). The RING Domain and the L79 Residue of Z Protein Are Involved in both the Rescue of Nucleocapsids and the Incorporation of Glycoproteins into Infectious Chimeric Arenavirus-Like Particles. J. Virol. 83: 7029-7039 [Abstract] [Full Text]  
  • Wilda, M., Lopez, N., Casabona, J. C., Franze-Fernandez, M. T. (2008). Mapping of the Tacaribe Arenavirus Z-Protein Binding Sites on the L Protein Identified both Amino Acids within the Putative Polymerase Domain and a Region at the N Terminus of L That Are Critically Involved in Binding. J. Virol. 82: 11454-11460 [Abstract] [Full Text]  
  • Sanchez, A. B., Perez, M., Cornu, T., de la Torre, J. C. (2005). RNA Interference-Mediated Virus Clearance from Cells both Acutely and Chronically Infected with the Prototypic Arenavirus Lymphocytic Choriomeningitis Virus. J. Virol. 79: 11071-11081 [Abstract] [Full Text]  
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