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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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