The NC domain of HIV-1 Gag contributes to the interaction of Gag with TSG101.

Fiche publication


Date publication

mars 2018

Journal

Biochimica et biophysica acta

Auteurs

Membres identifiés du Cancéropôle Est :
Pr MELY Yves, Dr RICHERT Ludovic


Tous les auteurs :
El Meshri SE, Boutant E, Mouhand A, Thomas A, Larue V, Richert L, Vivet-Boudou V, Mély Y, Tisné C, Muriaux D, de Rocquigny H

Résumé

HIV-1 Gag polyprotein orchestrates the assembly of viral particles. Its C-terminus consists of the nucleocapsid (NC) domain that interacts with RNA, and the p6 domain containing the PTAP motif that binds the cellular ESCRT factor TSG101 and ALIX. Deletion of the NC domain of Gag (GagNC) results in defective Gag assembly, a decrease in virus production and, thus probably affects recruitment of the ESCRT machinery. To investigate the role of GagNC in this recruitment, we analysed its impact on TSG101 and ALIX localisations and interactions in cells expressing Gag.

Mots clés

FRET, Gag, HIV, NMR, Nucleocapsid, TSG101

Référence

Biochim. Biophys. Acta. 2018 Mar 20;1862(6):1421-1431