Vaccinia virus hijacks ESCRT-mediated multivesicular body formation for virus egress.
ATPases Associated with Diverse Cellular Activities
/ metabolism
Cell Line
Endosomal Sorting Complexes Required for Transport
/ metabolism
Endosomes
/ virology
HeLa Cells
Humans
THP-1 Cells
Vaccinia virus
/ genetics
Vacuolar Proton-Translocating ATPases
/ metabolism
Viral Genome Packaging
Virus Release
Journal
Life science alliance
ISSN: 2575-1077
Titre abrégé: Life Sci Alliance
Pays: United States
ID NLM: 101728869
Informations de publication
Date de publication:
08 2021
08 2021
Historique:
received:
18
09
2020
revised:
03
06
2021
accepted:
04
06
2021
entrez:
19
6
2021
pubmed:
20
6
2021
medline:
15
12
2021
Statut:
epublish
Résumé
Poxvirus egress is a complex process whereby cytoplasmic single membrane-bound virions are wrapped in a cell-derived double membrane. These triple-membrane particles, termed intracellular enveloped virions (IEVs), are released from infected cells by fusion. Whereas the wrapping double membrane is thought to be derived from virus-modified trans-Golgi or early endosomal cisternae, the cellular factors that regulate virus wrapping remain largely undefined. To identify cell factors required for this process the prototypic poxvirus, vaccinia virus (VACV), was subjected to an RNAi screen directed against cellular membrane-trafficking proteins. Focusing on the endosomal sorting complexes required for transport (ESCRT), we demonstrate that ESCRT-III and VPS4 are required for packaging of virus into multivesicular bodies (MVBs). EM-based characterization of MVB-IEVs showed that they account for half of IEV production indicating that MVBs are a second major source of VACV wrapping membrane. These data support a model whereby, in addition to cisternae-based wrapping, VACV hijacks ESCRT-mediated MVB formation to facilitate virus egress and spread.
Identifiants
pubmed: 34145027
pii: 4/8/e202000910
doi: 10.26508/lsa.202000910
pmc: PMC8321658
pii:
doi:
Substances chimiques
Endosomal Sorting Complexes Required for Transport
0
Vacuolar Proton-Translocating ATPases
EC 3.6.1.-
ATPases Associated with Diverse Cellular Activities
EC 3.6.4.-
VPS4A protein, human
EC 3.6.4.6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Wellcome Trust
ID : 217202/Z/19/Z
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 102871/Z/13/Z
Pays : United Kingdom
Organisme : NIAID NIH HHS
ID : R37 AI051174
Pays : United States
Organisme : Medical Research Council
ID : MR/M02492X/1
Pays : United Kingdom
Organisme : Arthritis Research UK
ID : FC001076
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_UU12018/7
Pays : United Kingdom
Organisme : Cancer Research UK
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_UU_12018/7
Pays : United Kingdom
Organisme : Wellcome Trust
ID : WT102871MA
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_U12266B
Pays : United Kingdom
Informations de copyright
© 2021 Huttunen et al.
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