HBV Core Protein Is in Flux between Cytoplasmic, Nuclear, and Nucleolar Compartments.
CRM1
capsid
importin
nucleolar retention
nucleolin
virus assembly
Journal
mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231
Informations de publication
Date de publication:
09 02 2021
09 02 2021
Historique:
entrez:
10
2
2021
pubmed:
11
2
2021
medline:
27
8
2021
Statut:
epublish
Résumé
Hepatitis B virus (HBV) core protein (Cp) can be found in the nucleus and cytoplasm of infected hepatocytes; however, it preferentially segregates to a specific compartment correlating with disease status. Regulation of this intracellular partitioning of Cp remains obscure. In this paper, we report that cellular compartments are filled and vacated by Cp in a time- and concentration-dependent manner in both transfections and infections. At early times after transfection, Cp, in a dimeric state, preferentially localizes to the nucleolus. Later, the nucleolar compartment is emptied and Cp progresses to being predominantly nuclear, with a large fraction of the protein in an assembled state. Nuclear localization is followed by cell-wide distribution, and then Cp becomes exclusively cytoplasmic. The same trend in Cp movement is seen during an infection. Putative nucleolar retention signals have been identified and appear to be structure dependent. Export of Cp from the nucleus involves the CRM1 exportin. Time-dependent flux can be recapitulated by modifying Cp concentration, suggesting transitions are regulated by reaching a threshold concentration.
Identifiants
pubmed: 33563815
pii: mBio.03514-20
doi: 10.1128/mBio.03514-20
pmc: PMC8545122
pii:
doi:
Substances chimiques
Antiviral Agents
0
DNA, Viral
0
Viral Core Proteins
0
Viral Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIAID NIH HHS
ID : R01 AI144022
Pays : United States
Informations de copyright
Copyright © 2021 Nair and Zlotnick.
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