UBE2O, a host ubiquitin-conjugating enzyme, is a key regulator of hepatitis B virus maturation and egress

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00640457" target="_blank" >RIV/61388963:_____/25:00640457 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/25:10503868

Result on the web

<a href="https://doi.org/10.1016/j.jbc.2025.110750" target="_blank" >https://doi.org/10.1016/j.jbc.2025.110750</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jbc.2025.110750" target="_blank" >10.1016/j.jbc.2025.110750</a>

Result language

angličtina

Original language name

UBE2O, a host ubiquitin-conjugating enzyme, is a key regulator of hepatitis B virus maturation and egress

Original language description

A critical step in Hepatitis B virus (HBV) maturation and egress is the ubiquitination of the capsid/core protein (HBc), which enables its recognition by the endosomal sorting complex required for transport (ESCRT) machinery and recruitment to multivesicular bodies (MVBs). This study investigates the role of UBE2O, an atypical E2 ubiquitin-conjugating enzyme with intrinsic E3 ligase activity, in nucleocapsid assembly and virion egress. Loss of UBE2O in HBV-infected primary human hepatocytes (PHH) and HepG2-NTCP cells led to a reduction in viral replication, as evidenced by decreased levels of intracellular HBV DNA, pgRNA, capsids, and extracellular HBeAg. Additionally, UBE2O depletion disrupted intracellular nucleocapsid assembly and impaired the secretion of enveloped virions, but the release of naked nucleocapsids remained unaffected. In contrast, UBE2O overexpression enhanced the secretion of mature virions, whereas the expression of its enzymatically inactive mutant inhibited this process. Additionally, UBE2O mediated the monoubiquitination of hypophosphorylated cytoplasmic HBc and capsids. Subcellular localization experiments using confocal microscopy and proximity ligation assays (PLA) demonstrated that UBE2O colocalizes with capsids and ubiquitinated cargo in CD63-positive MVB compartments, indicating its involvement in the endosomal secretory pathway. Collectively, this study identifies UBE2O and its catalytic activity as key regulators of the HBV virion secretion pathway, highlighting its potential as a therapeutic target for HBV treatment.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10607 - Virology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2025

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

1083-351X

Volume of the periodical

301

Issue of the periodical within the volume

11

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

24

Pages from-to

110750

UT code for WoS article

001602642200001

EID of the result in the Scopus database

2-s2.0-105018857907