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

Viruses. 2020 Sep 29;12(10):1109. doi: 10.3390/v12101109.

Abstract

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.

Keywords: HIV-1; NMR; RNA; RNA-binding protein; nucleic acids; nucleocapsid.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • DNA-Binding Proteins
  • Endosomal Sorting Complexes Required for Transport
  • HIV-1 / genetics
  • HIV-1 / metabolism*
  • Nucleic Acids / chemistry*
  • Nucleocapsid / metabolism
  • Nucleocapsid Proteins / metabolism*
  • Protein Binding
  • RNA, Viral
  • Transcription Factors
  • Virion / metabolism
  • gag Gene Products, Human Immunodeficiency Virus / chemistry
  • gag Gene Products, Human Immunodeficiency Virus / metabolism

Substances

  • DNA-Binding Proteins
  • Endosomal Sorting Complexes Required for Transport
  • NCP7 protein, Human immunodeficiency virus 1
  • Nucleic Acids
  • Nucleocapsid Proteins
  • RNA, Viral
  • Transcription Factors
  • Tsg101 protein
  • gag Gene Products, Human Immunodeficiency Virus
  • p15 gag protein, Human immunodeficiency virus 1