viruses Review How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain 1 2, 2, 2 1 Jéromine Klingler , Halina Anton y, Eléonore Réal y, Manon Zeiger , Christiane Moog , Yves Mély 2 and Emmanuel Boutant 2,* 1 INSERM UMR_S 1109, Centre de Recherche en Immunologie et Hématologie, Faculté de Médecine, Université de Strasbourg, 67000 Strasbourg, France;
[email protected] (J.K.);
[email protected] (C.M.) 2 UMR 7021, CNRS, Laboratoire de Bioimagerie et Pathologies, Université de Strasbourg, Faculté de Pharmacie, 67400 Illkirch, France;
[email protected] (H.A.);
[email protected] (E.R.);
[email protected] (M.Z.);
[email protected] (Y.M.) * Correspondence:
[email protected] These authors contributed equally to this work. y Received: 13 July 2020; Accepted: 10 August 2020; Published: 13 August 2020 Abstract: The human immunodeficiency virus (HIV-1) polyprotein Gag (Group-specific antigen) plays a central role in controlling the late phase of the viral lifecycle. Considered to be only a scaffolding protein for a long time, the structural protein Gag plays determinate and specific roles in HIV-1 replication. Indeed, via its different domains, Gag orchestrates the specific encapsidation of the genomic RNA, drives the formation of the viral particle by its auto-assembly (multimerization), binds multiple viral proteins, and interacts with a large number of cellular proteins that are needed for its functions from its translation location to the plasma membrane, where newly formed virions are released. Here, we review the interactions between HIV-1 Gag and 66 cellular proteins.