Vaccinia virus E3 prevents sensing of Z-RNA to block ZBP1-dependent necroptosis.
DAI
E3L
VACV
Z-DNA-binding domain
Z-RNA
Z-form nucleic acid
ZBP1
cell death
necroptosis
poxvirus
Journal
Cell host & microbe
ISSN: 1934-6069
Titre abrégé: Cell Host Microbe
Pays: United States
ID NLM: 101302316
Informations de publication
Date de publication:
11 Aug 2021
11 Aug 2021
Historique:
received:
15
10
2020
revised:
02
04
2021
accepted:
18
05
2021
pubmed:
1
7
2021
medline:
15
12
2021
entrez:
30
6
2021
Statut:
ppublish
Résumé
Necroptosis mediated by Z-nucleic-acid-binding protein (ZBP)1 (also called DAI or DLM1) contributes to innate host defense against viruses by triggering cell death to eliminate infected cells. During infection, vaccinia virus (VACV) protein E3 prevents death signaling by competing for Z-form RNA through an N-terminal Zα domain. In the absence of this E3 domain, Z-form RNA accumulates during the early phase of VACV infection, triggering ZBP1 to recruit receptor interacting protein kinase (RIPK)3 and execute necroptosis. The C-terminal E3 double-strand RNA-binding domain must be retained to observe accumulation of Z-form RNA and induction of necroptosis. Substitutions of Zα from either ZBP1 or the RNA-editing enzyme double-stranded RNA adenosine deaminase (ADAR)1 yields fully functional E3 capable of suppressing virus-induced necroptosis. Overall, our evidence reveals the importance of Z-form RNA generated during VACV infection as a pathogen-associated molecular pattern (PAMP) unleashing ZBP1/RIPK3/MLKL-dependent necroptosis unless suppressed by viral E3.
Identifiants
pubmed: 34192517
pii: S1931-3128(21)00237-7
doi: 10.1016/j.chom.2021.05.009
pmc: PMC9333947
mid: NIHMS1722942
pii:
doi:
Substances chimiques
E3L protein, Vaccinia virus
0
RNA, Double-Stranded
0
RNA-Binding Proteins
0
Viral Proteins
0
ZBP1 protein, human
0
MLKL protein, human
EC 2.7.-
Protein Kinases
EC 2.7.-
RIPK3 protein, human
EC 2.7.11.1
Receptor-Interacting Protein Serine-Threonine Kinases
EC 2.7.11.1
ADAR protein, human
EC 3.5.4.37
Adenosine Deaminase
EC 3.5.4.4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1266-1276.e5Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK074731
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI095394
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI135025
Pays : United States
Organisme : NIDDK NIH HHS
ID : R56 DK074731
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI020211
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA006927
Pays : United States
Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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