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Journal of Virology, May 2001, p. 4367-4375, Vol. 75, No. 9
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.9.4367-4375.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Human Foamy Virus Capsid Formation Requires an Interaction Domain in the N Terminus of Gag

Joelle Tobaly-Tapiero, Patricia Bittoun, Marie-Lou Giron, Manuel Neves, Marcel Koken, Ali Saïb,* and Hugues de Thé

CNRS UPR9051, Hôpital Saint-Louis, Université Paris 7, 75475 Paris Cedex 10, France

Received 26 October 2000/Accepted 6 February 2001

Retroviral Gag expression is sufficient for capsid assembly, which occurs through interaction between distinct Gag domains. Human foamy virus (HFV) capsids assemble within the cytoplasm, although their budding, which mainly occurs in the endoplasmic reticulum, requires the presence of homologous Env. Yet little is known about the molecular basis of HFV Gag precursor assembly. Using fusions between HFV Gag and a nuclear reporter protein, we have identified a strong interaction domain in the N terminus of HFV Gag which is predicted to contain a conserved coiled-coil motif. Deletion within this region in an HFV provirus abolishes viral production through inhibition of capsid assembly.

* Corresponding author. Mailing address: CNRS UPR9051, Hôpital Saint-Louis, 1, Ave. Claude Vellefaux, 75475 Paris Cedex 10, France. Phone: 33.1.53.72.40.96. Fax: 33.1.53.72.40.90. E-mail: alisaib{at}infobiogen.fr.

Journal of Virology, May 2001, p. 4367-4375, Vol. 75, No. 9
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.9.4367-4375.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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