TRIM26 positively affects hepatitis B virus replication by inhibiting proteasome-dependent degradation of viral core protein.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
21 08 2023
21 08 2023
Historique:
received:
23
03
2023
accepted:
16
08
2023
medline:
23
8
2023
pubmed:
22
8
2023
entrez:
21
8
2023
Statut:
epublish
Résumé
Chronic hepatitis B virus (HBV) infection is a major medical concern worldwide. Current treatments for HBV infection effectively inhibit virus replication; however, these treatments cannot cure HBV and novel treatment-strategies should be necessary. In this study, we identified tripartite motif-containing protein 26 (TRIM26) could be a supportive factor for HBV replication. Small interfering RNA-mediated TRIM26 knockdown (KD) modestly attenuated HBV replication in human hepatocytes. Endogenous TRIM26 physically interacted with HBV core protein (HBc), but not polymerase and HBx, through the TRIM26 SPRY domain. Unexpectedly, TRIM26 inhibited HBc ubiquitination even though TRIM26 is an E3 ligase. HBc was degraded by TRIM26 KD in Huh-7 cells, whereas the reduction was restored by a proteasome inhibitor. RING domain-deleted TRIM26 mutant (TRIM26ΔR), a dominant negative form of TRIM26, sequestered TRIM26 from HBc, resulting in promoting HBc degradation. Taking together, this study demonstrated that HBV utilizes TRIM26 to avoid the proteasome-dependent HBc degradation. The interaction between TRIM26 and HBc might be a novel therapeutic target against HBV infection.
Identifiants
pubmed: 37604854
doi: 10.1038/s41598-023-40688-3
pii: 10.1038/s41598-023-40688-3
pmc: PMC10442393
doi:
Substances chimiques
Proteasome Endopeptidase Complex
EC 3.4.25.1
Viral Core Proteins
0
TRIM26 protein, human
EC 2.3.2.27
Tripartite Motif Proteins
0
Ubiquitin-Protein Ligases
EC 2.3.2.27
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
13584Informations de copyright
© 2023. Springer Nature Limited.
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