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- W3048535337 endingPage "888" @default.
- W3048535337 startingPage "888" @default.
- W3048535337 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. Notably, we describe the techniques used to evidence these interactions, the different domains of Gag involved, and the implications of these interactions in the HIV-1 replication cycle. In the final part, we focus on the interactions involving the highly conserved nucleocapsid (NC) domain of Gag and detail the functions of the NC interactants along the viral lifecycle." @default.
- W3048535337 created "2020-08-18" @default.
- W3048535337 creator A5034557642 @default.
- W3048535337 creator A5035136737 @default.
- W3048535337 creator A5057462377 @default.
- W3048535337 creator A5061303801 @default.
- W3048535337 creator A5070213528 @default.
- W3048535337 creator A5074948769 @default.
- W3048535337 creator A5080751117 @default.
- W3048535337 date "2020-08-13" @default.
- W3048535337 modified "2023-09-27" @default.
- W3048535337 title "How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain" @default.
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