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Journal of Virology, June 2001, p. 5277-5287, Vol. 75, No. 11
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.11.5277-5287.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The NH2-Terminal Domain of the Human T-Cell Leukemia Virus Type 1 Capsid Protein Is Involved in Particle Formation

Fabienne Rayne, Fadila Bouamr, Jacqueline Lalanne, and Robert Z. Mamoun*

INSERM U443, Equipe Rétrovirus et Transfert Génique, Université Victor Segalen Bordeaux 2, F-33076 Bordeaux Cedex, France

Received 8 January 2001/Accepted 2 March 2001

The human immunodeficiency virus type 1 (HIV-1) and human T-cell leukemia virus type 1 (HTLV-1) capsid proteins (CA) display similar structures formed by two independently folded N-terminal (NTD) and C-terminal (CTD) domains. To characterize the functions harbored by the HTLV-1 CA domains in particle formation, 12 sites scattered throughout the protein were mutated. The effects of the mutations on Gag membrane binding, proteolytic processing, and virus-like particle secretion were analyzed. It appears that the NTD is the major partner of indirect or direct Gag-Gag interactions. In particular, most of the NTD mutations impaired virion morphogenesis, and no mutation located in the NTD could be fully rescued by coexpression of wild-type Gag. In contrast, the CTD seems not to be involved in Gag-Gag interactions. Nevertheless, an unknown function required for particle formation is located in the CTD. Thus, despite an overall structural similarity between the HIV-1 and HTLV-1 CA proteins, their NTDs and CTDs exhibit different functions.

* Corresponding author. Mailing address: INSERM U443, Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, F-33076 Bordeaux Cedex, France. Phone: (33) 5 57 57 11 15. Fax: (33) 5 57 57 11 90. E-mail: robert.mamoun{at}retrovirether.u-bordeaux2.fr.

Journal of Virology, June 2001, p. 5277-5287, Vol. 75, No. 11
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.11.5277-5287.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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