The life-cycle of the HIV-1 Gag–RNA complex
E Mailler, S Bernacchi, R Marquet, JC Paillart… - Viruses, 2016 - mdpi.com
Human immunodeficiency virus type 1 (HIV-1) replication is a highly regulated process
requiring the recruitment of viral and cellular components to the plasma membrane for …
requiring the recruitment of viral and cellular components to the plasma membrane for …
The interplay between ESCRT and viral factors in the enveloped virus life cycle
B Meng, AML Lever - Viruses, 2021 - mdpi.com
Viruses are obligate parasites that rely on host cellular factors to replicate and spread. The
endosomal sorting complexes required for transport (ESCRT) system, which is classically …
endosomal sorting complexes required for transport (ESCRT) system, which is classically …
[HTML][HTML] Scaffolding viral protein NC nucleates phase separation of the HIV-1 biomolecular condensate
A Monette, M Niu, MN Asser, RJ Gorelick, AJ Mouland - Cell Reports, 2022 - cell.com
Membraneless biomolecular condensates (BMCs) contribute to the replication of a growing
number of viruses but remain to be functionally characterized. Previously, we demonstrated …
number of viruses but remain to be functionally characterized. Previously, we demonstrated …
Nucleocapsid protein: a desirable target for future therapies against HIV-1
HIV reverse transcription and nucleocapsid. After the capsid has entered the cell, reverse
transcriptase (A) creates a DNA copy (green) of the HIV RNA genome (yellow), using a …
transcriptase (A) creates a DNA copy (green) of the HIV RNA genome (yellow), using a …
The C-terminal p6 domain of the HIV-1 Pr55Gag precursor is required for specific binding to the genomic RNA
N Dubois, KK Khoo, S Ghossein, T Seissler, P Wolff… - RNA biology, 2018 - Taylor & Francis
ABSTRACT The Pr55Gag precursor specifically selects the HIV-1 genomic RNA (gRNA)
from a large excess of cellular and partially or fully spliced viral RNAs and drives the virus …
from a large excess of cellular and partially or fully spliced viral RNAs and drives the virus …
The thermodynamics of Pr55Gag-RNA interaction regulate the assembly of HIV
HS Tanwar, KK Khoo, M Garvey, L Waddington… - PLoS …, 2017 - journals.plos.org
The interactions that occur during HIV Pr55Gag oligomerization and genomic RNA
packaging are essential elements that facilitate HIV assembly. However, mechanistic details …
packaging are essential elements that facilitate HIV assembly. However, mechanistic details …
Overview of the nucleic-acid binding properties of the HIV-1 nucleocapsid protein in its different maturation states
A Mouhand, M Pasi, M Catala, L Zargarian, A Belfetmi… - Viruses, 2020 - mdpi.com
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 …
the nucleocapsid (NC) domain that interacts with nucleic acids, and p1 and p6, two …
Structural maturation of the HIV-1 RNA 5' untranslated region by Pr55Gag and its maturation products
O Gilmer, E Mailler, JC Paillart, A Mouhand, C Tisné… - RNA biology, 2022 - Taylor & Francis
Maturation of the HIV-1 viral particles shortly after budding is required for infectivity. During
this process, the Pr55Gag precursor undergoes a cascade of proteolytic cleavages, and …
this process, the Pr55Gag precursor undergoes a cascade of proteolytic cleavages, and …
Elucidation of the molecular mechanism driving duplication of the HIV-1 PTAP late domain
AN Martins, AA Waheed, SD Ablan, W Huang… - Journal of …, 2016 - Am Soc Microbiol
ABSTRACT HIV-1 uses cellular machinery to bud from infected cells. This cellular machinery
is comprised of several multiprotein complexes known as endosomal sorting complexes …
is comprised of several multiprotein complexes known as endosomal sorting complexes …
The nucleic acid chaperone activity of the HIV-1 Gag polyprotein is boosted by its cellular partner RPL7: a kinetic study
H Karnib, MF Nadeem, N Humbert… - Nucleic acids …, 2020 - academic.oup.com
The HIV-1 Gag protein playing a key role in HIV-1 viral assembly has recently been shown
to interact through its nucleocapsid domain with the ribosomal protein L7 (RPL7) that acts as …
to interact through its nucleocapsid domain with the ribosomal protein L7 (RPL7) that acts as …