HIV-1 Envelope Overcomes NLRP3-Mediated Inhibition of F-Actin Polymerization for Viral Entry.
CBL
HIV
NLRP3
P2Y2
inflammasome
viral entry
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
24 09 2019
24 09 2019
Historique:
received:
27
06
2018
revised:
08
01
2019
accepted:
22
02
2019
entrez:
26
9
2019
pubmed:
26
9
2019
medline:
21
10
2020
Statut:
ppublish
Résumé
Purinergic receptors and nucleotide-binding domain leucine-rich repeat containing (NLR) proteins have been shown to control viral infection. Here, we show that the NLR family member NLRP3 and the purinergic receptor P2Y2 constitutively interact and regulate susceptibility to HIV-1 infection. We found that NLRP3 acts as an inhibitory factor of viral entry that represses F-actin remodeling. The binding of the HIV-1 envelope to its host cell receptors (CD4, CXCR4, and/or CCR5) overcomes this restriction by stimulating P2Y2. Once activated, P2Y2 enhances its interaction with NLRP3 and stimulates the recruitment of the E3 ubiquitin ligase CBL to NLRP3, ultimately leading to NLRP3 degradation. NLRP3 degradation is permissive for PYK2 phosphorylation (PYK2Y402
Identifiants
pubmed: 31553908
pii: S2211-1247(19)30281-5
doi: 10.1016/j.celrep.2019.02.095
pii:
doi:
Substances chimiques
Actins
0
NLR Family, Pyrin Domain-Containing 3 Protein
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
3381-3394.e7Informations de copyright
Copyright © 2019 The Author(s). Published by Elsevier Inc. All rights reserved.