Herpes Simplex Virus Organizes Cytoplasmic Membranes To Form a Viral Assembly Center in Neuronal Cells.
Actin Cytoskeleton
/ metabolism
Animals
Capsid
/ metabolism
Capsid Proteins
/ metabolism
Cell Line
Cell Membrane
/ metabolism
Chlorocebus aethiops
Cytoplasm
/ virology
Golgi Apparatus
/ metabolism
Herpes Simplex
/ virology
Herpesvirus 1, Human
/ genetics
Neurons
/ virology
Vero Cells
Viral Proteins
/ metabolism
Viral Structural Proteins
/ metabolism
Virion
/ metabolism
Virus Assembly
/ physiology
herpes simplex virus
membrane trafficking
virus assembly
virus envelopment
Journal
Journal of virology
ISSN: 1098-5514
Titre abrégé: J Virol
Pays: United States
ID NLM: 0113724
Informations de publication
Date de publication:
15 09 2020
15 09 2020
Historique:
received:
08
05
2020
accepted:
15
07
2020
pubmed:
24
7
2020
medline:
22
12
2020
entrez:
24
7
2020
Statut:
epublish
Résumé
Herpes simplex virus (HSV) is a neuroinvasive virus that has been used as a model organism for studying common properties of all herpesviruses. HSV induces host organelle rearrangement and forms multiple, dispersed assembly compartments in epithelial cells, which complicates the study of HSV assembly. In this study, we show that HSV forms a visually distinct unitary cytoplasmic viral assembly center (cVAC) in both cancerous and primary neuronal cells that concentrates viral structural proteins and is a major site of capsid envelopment. The HSV cVAC also concentrates host membranes that are important for viral assembly, such as Golgi- and recycling endosome-derived membranes. Finally, we show that HSV cVAC formation and/or maintenance depends on an intact microtubule network and a viral tegument protein, pUL51. Our observations suggest that the neuronal cVAC is a uniquely useful model to study common herpesvirus assembly pathways and cell-specific pathways for membrane reorganization.
Identifiants
pubmed: 32699089
pii: JVI.00900-20
doi: 10.1128/JVI.00900-20
pmc: PMC7495378
pii:
doi:
Substances chimiques
Capsid Proteins
0
Viral Proteins
0
Viral Structural Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NCI NIH HHS
ID : P30 CA086862
Pays : United States
Organisme : NIAID NIH HHS
ID : R21 AI133155
Pays : United States
Organisme : NIAID NIH HHS
ID : R21 AI153683
Pays : United States
Informations de copyright
Copyright © 2020 American Society for Microbiology.
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