1H, 13C and 15N backbone and partial side-chain resonance assignments of the C-terminal domain of HIV-1 Pr55Gag encompassed in NCp15

Valéry Larue; Marjorie Catala; Anissa Belfetmi; Loussiné Zargarian; Olivier Mauffret; Carine Tisné

doi:10.1007/s12104-017-9796-x

¹H, ¹³C and ¹⁵N backbone and partial side-chain resonance assignments of the C-terminal domain of HIV-1 Pr55^Gag encompassed in NCp15

Biomol NMR Assign. 2018 Apr;12(1):139-143. doi: 10.1007/s12104-017-9796-x. Epub 2018 Jan 13.

Authors

Valéry Larue¹, Marjorie Catala^{2

3}, Anissa Belfetmi⁴, Loussiné Zargarian⁴, Olivier Mauffret⁴, Carine Tisné^{5

6}

Affiliations

¹ Laboratoire de Cristallographie et RMN Biologiques, CNRS UMR 8015, Faculté de Pharmacie, Université Paris Descartes, USPC, 4 avenue de l'Observatoire, 75006, Paris, France. [email protected].
² Laboratoire de Cristallographie et RMN Biologiques, CNRS UMR 8015, Faculté de Pharmacie, Université Paris Descartes, USPC, 4 avenue de l'Observatoire, 75006, Paris, France.
³ Laboratoire d'Expression génétique microbienne, IBPC, CNRS UMR 8261, USPC, 13 rue Pierre et Marie Curie, 75005, Paris, France.
⁴ LBPA, CNRS UMR 8113, ENS Paris-Saclay, Université Paris-Saclay, 61 Avenue du Pdt Wilson, F-94235, Cachan, France.
⁵ Laboratoire de Cristallographie et RMN Biologiques, CNRS UMR 8015, Faculté de Pharmacie, Université Paris Descartes, USPC, 4 avenue de l'Observatoire, 75006, Paris, France. [email protected].
⁶ Laboratoire d'Expression génétique microbienne, IBPC, CNRS UMR 8261, USPC, 13 rue Pierre et Marie Curie, 75005, Paris, France. [email protected].

PMID: 29332151
DOI: 10.1007/s12104-017-9796-x

Abstract

During HIV-1 assembly, the Pr55^Gag polyprotein precursor (Gag) interacts with the genomic RNA, with lipids of the plasma membrane, with host proteins (ALIX, TSG101) through the ESCRT complex, with the viral protein Vpr and are involved in intermolecular interactions with other Pr55^Gag proteins. This network of interactions is responsible for the formation of the viral particle, the selection of genomic RNA and the packaging of Vpr. The C-terminal domain of Gag encompassed in NCp15 is involved in the majority of these interactions, either by its nucleocapsid or its p6 domains. We study the NCp15 protein as a model of the C-terminal domain of Gag to better understand the role of this domain in the assembly and budding of HIV-1. Here, we report the ¹H, ¹³C and ¹⁵N chemical shift assignments of NCp15 obtained by heteronuclear multidimensional NMR spectroscopy as well as the analysis of its secondary structure in solution. These assignments of NCp15 pave the way for interaction studies with its numerous partners.

Keywords: HIV-1; NCp15; NMR; Nucleocapsid; Resonance assignment.

Publication types

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

MeSH terms

Nuclear Magnetic Resonance, Biomolecular*
Protein Domains
Protein Precursors / chemistry*

Substances

Protein Precursors
p55 gag precursor protein, Human immunodeficiency virus 1