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 Capul, A. A.
Right arrow Articles by de la Torre, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Capul, A. A.
Right arrow Articles by de la Torre, J. C.

 Previous Article  |  Next Article 

Journal of Virology, September 2007, p. 9451-9460, Vol. 81, No. 17
0022-538X/07/$08.00+0     doi:10.1128/JVI.00499-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Arenavirus Z-Glycoprotein Association Requires Z Myristoylation but Not Functional RING or Late Domains{triangledown}

Althea A. Capul, Mar Perez, Emily Burke, Stefan Kunz, Michael J. Buchmeier, and Juan C. de la Torre*

Molecular and Integrative Neuroscience Department (MIND), Scripps Research Institute, La Jolla, California 92037

Received 8 March 2007/ Accepted 13 June 2007

Generation of infectious arenavirus-like particles requires the virus RING finger Z protein and surface glycoprotein precursor (GPC) and the correct processing of GPC into GP1, GP2, and a stable signal peptide (SSP). Z is the driving force of arenavirus budding, whereas the GP complex (GPc), consisting of hetero-oligomers of SSP, GP1, and GP2, forms the viral envelope spikes that mediate receptor recognition and cell entry. Based on the roles played by Z and GP in the arenavirus life cycle, we hypothesized that Z and the GPc should interact in a manner required for virion formation. Here, using confocal microscopy and coimmunoprecipitation assays, we provide evidence for subcellular colocalization and biochemical interaction, respectively, of Z and the GPc. Our results from mutation-function analysis reveal that Z myristoylation, but not the Z late (L) or RING domain, is required for Z-GPc interaction. Moreover, Z interacted directly with SSP in the absence of other components of the GPc. We obtained similar results with Z and GPC from the prototypical arenavirus lymphocytic choriomeningitis virus and the hemorrhagic fever arenavirus Lassa fever virus.


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

{triangledown} Published ahead of print on 20 June 2007.


Journal of Virology, September 2007, p. 9451-9460, Vol. 81, No. 17
0022-538X/07/$08.00+0     doi:10.1128/JVI.00499-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Agnihothram, S. S., Dancho, B., Grant, K. W., Grimes, M. L., Lyles, D. S., Nunberg, J. H. (2009). Assembly of Arenavirus Envelope Glycoprotein GPC in Detergent-Soluble Membrane Microdomains. J. Virol. 83: 9890-9900 [Abstract] [Full Text]  
  • 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]  
  • Cosset, F.-L., Marianneau, P., Verney, G., Gallais, F., Tordo, N., Pecheur, E.-I., ter Meulen, J., Deubel, V., Bartosch, B. (2009). Characterization of Lassa Virus Cell Entry and Neutralization with Lassa Virus Pseudoparticles. J. Virol. 83: 3228-3237 [Abstract] [Full Text]