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.
Highlights
The human immunodeficiency virus (HIV-1) genome encodes three major polyproteins: Gag, Pol and Env, two regulatory proteins: Tat and Rev as well as four accessory proteins: Vif, Vpu, Vpr and Nef
It corresponds to the 52 amino acids located at the C-terminus of the Gag polyprotein and contains several conserved motifs involved in the interactions with viral (Vpr) and cellular proteins (Tsg101, ALIX, ERK-2, aPKC)
Data presented in this table are as follows: cellular partner implicated in the interaction, classification of the interacting protein, the role of the protein, Gag domain involved in the interaction, the potential function of the complex during HIV-1 viral replication, experiments used to demonstrate the interaction and, references related to the interaction
Summary
The human immunodeficiency virus (HIV-1) genome encodes three major polyproteins: Gag (group-specific antigen), Pol (polymerase) and Env (envelope), two regulatory proteins: Tat (transactivator of transcription) and Rev (regulator of virion expression) as well as four accessory proteins: Vif (virion infectivity factor), Vpu (viral protein u), Vpr (viral protein r) and Nef (negative regulatory factor). The mature Gag plays crucial functions in HIV-1 replication, notably during the assembly, budding, and release of infectious particles [1,2,3]. The MA domain is implicated in the targeting and binding of Gag to the plasma membrane (PM) It binds RNAs and mediates the incorporation of Env in virions. HIV-1 assembly takes place at the PM [4,5] or at a specific intracellular location named virus-containing compartment (VCC), which are PM invaginations in the cytoplasm, initially thought to be late endosomal structures in Viruses 2020, 12, x FOR PEER REVIEW macrophages [5,6,7,8,9,10,11]. The viral budding and release are synchronized with the activation of the viral protease which
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