Overview of the Nucleic-Acid Binding Properties of the HIV-1 Nucleocapsid Protein in Its Different Maturation States

Overview of the Nucleic-Acid Binding Properties of the HIV-1 Nucleocapsid Protein in Its Different Maturation States

HIV-1 Gag polyprotein orchestrates the assembly of viral particles. Its C-terminus consists of the nucleocapsid (NC) domain that interacts with nucleic acids, and p1 and p6, two unstructured regions, p6 containing the motifs to bind ALIX, the cellular ESCRT factor TSG101 and the viral protein Vpr. T...

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Bibliographic Details
Main Authors: Assia Mouhand, Marco Pasi, Marjorie Catala, Loussiné Zargarian, Anissa Belfetmi, Pierre Barraud, Olivier Mauffret, Carine Tisné
Format: Article
Language:English
Published: MDPI AG 2020-09-01
Series:Viruses
Subjects:
HIV-1
nucleocapsid
nucleic acids
RNA
RNA-binding protein
NMR
Online Access:https://www.mdpi.com/1999-4915/12/10/1109
Description
Summary:HIV-1 Gag polyprotein orchestrates the assembly of viral particles. Its C-terminus consists of the nucleocapsid (NC) domain that interacts with nucleic acids, and p1 and p6, two unstructured regions, p6 containing the motifs to bind ALIX, the cellular ESCRT factor TSG101 and the viral protein Vpr. The processing of Gag by the viral protease subsequently liberates NCp15 (NC-p1-p6), NCp9 (NC-p1) and NCp7, NCp7 displaying the optimal chaperone activity of nucleic acids. This review focuses on the nucleic acid binding properties of the NC domain in the different maturation states during the HIV-1 viral cycle.
ISSN:1999-4915

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