Host factor heat-shock protein 90 contributes to baculovirus budded virus morphogenesis via facilitating nuclear actin polymerization.
BV morphogenesis
Baculovirus
F-actin
Hsp90
Regulatory mechanism
Journal
Virology
ISSN: 1096-0341
Titre abrégé: Virology
Pays: United States
ID NLM: 0110674
Informations de publication
Date de publication:
09 2019
09 2019
Historique:
received:
25
02
2019
revised:
03
07
2019
accepted:
04
07
2019
pubmed:
19
7
2019
medline:
9
4
2020
entrez:
19
7
2019
Statut:
ppublish
Résumé
Hsp90, a highly conserved cellular molecular chaperone, is involved in the life cycle of many viruses. A recent proteomics study revealed that Hsp90 was incorporated into the budded virions (BVs) of baculovirus, we therefore explored the role of Hsp90 during Autographa californica multiple nucleopolyhedrovirus (AcMNPV) infection process. The results showed that Hsp90 was essential for AcMNPV BV propagation in cultured cells. Electron microscopy detected that nucleocapsids failed to egress from the nucleus to the cytoplasm for further BV budding. Inactivation of Hsp90 abolished virus-triggered nuclear actin polymerization, a process providing essential driving forces for nucleocapsid egress. Further analyses suggested that this was due to the selectively regulation of the proper protein levels and nuclear accumulation of P40 subunit of host actin related protein 2/3 complex (Arp2/3). Thus, Hsp90 participates in baculovirus BV propagation by facilitating nuclear actin polymerization required for progeny BV production.
Identifiants
pubmed: 31319277
pii: S0042-6822(19)30181-3
doi: 10.1016/j.virol.2019.07.006
pii:
doi:
Substances chimiques
Actins
0
HSP90 Heat-Shock Proteins
0
Nuclear Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
200-209Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.