PMID- 37604854
OWN - NLM
STAT- MEDLINE
DCOM- 20230823
LR  - 20231121
IS  - 2045-2322 (Electronic)
IS  - 2045-2322 (Linking)
VI  - 13
IP  - 1
DP  - 2023 Aug 21
TI  - TRIM26 positively affects hepatitis B virus replication by inhibiting 
      proteasome-dependent degradation of viral core protein.
PG  - 13584
LID - 10.1038/s41598-023-40688-3 [doi]
LID - 13584
AB  - 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 (TRIM26DeltaR), 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.
CI  - (c) 2023. Springer Nature Limited.
FAU - Nakaya, Yuki
AU  - Nakaya Y
AD  - Division of Virology, Department of Infection and Immunity, Jichi Medical 
      University, Shimotsuke, 329-0498, Japan. nakaya.yuki@jichi.ac.jp.
FAU - Nishizawa, Tsutomu
AU  - Nishizawa T
AD  - Division of Virology, Department of Infection and Immunity, Jichi Medical 
      University, Shimotsuke, 329-0498, Japan.
FAU - Nishitsuji, Hironori
AU  - Nishitsuji H
AD  - Department of Virology and Parasitology, School of Medicine, Fujita Health 
      University, Toyoake, 470-1192, Japan.
FAU - Morita, Hiromi
AU  - Morita H
AD  - Division of Virology, Department of Infection and Immunity, Jichi Medical 
      University, Shimotsuke, 329-0498, Japan.
FAU - Yamagata, Tomoko
AU  - Yamagata T
AD  - Division of Virology, Department of Infection and Immunity, Jichi Medical 
      University, Shimotsuke, 329-0498, Japan.
FAU - Onomura, Daichi
AU  - Onomura D
AD  - Division of Virology, Department of Infection and Immunity, Jichi Medical 
      University, Shimotsuke, 329-0498, Japan.
FAU - Murata, Kazumoto
AU  - Murata K
AD  - Division of Virology, Department of Infection and Immunity, Jichi Medical 
      University, Shimotsuke, 329-0498, Japan. kmurata@jichi.ac.jp.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20230821
PL  - England
TA  - Sci Rep
JT  - Scientific reports
JID - 101563288
RN  - EC 3.4.25.1 (Proteasome Endopeptidase Complex)
RN  - 0 (Viral Core Proteins)
RN  - EC 2.3.2.27 (TRIM26 protein, human)
RN  - 0 (Tripartite Motif Proteins)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
SB  - IM
MH  - Humans
MH  - Hepatitis B virus/genetics
MH  - *Hepatitis B, Chronic
MH  - Proteasome Endopeptidase Complex
MH  - *Hepatitis B
MH  - Viral Core Proteins/genetics
MH  - Tripartite Motif Proteins/genetics
MH  - Ubiquitin-Protein Ligases/genetics
PMC - PMC10442393
COIS- The authors declare no competing interests.
EDAT- 2023/08/22 00:41
MHDA- 2023/08/23 06:42
PMCR- 2023/08/21
CRDT- 2023/08/21 23:26
PHST- 2023/03/23 00:00 [received]
PHST- 2023/08/16 00:00 [accepted]
PHST- 2023/08/23 06:42 [medline]
PHST- 2023/08/22 00:41 [pubmed]
PHST- 2023/08/21 23:26 [entrez]
PHST- 2023/08/21 00:00 [pmc-release]
AID - 10.1038/s41598-023-40688-3 [pii]
AID - 40688 [pii]
AID - 10.1038/s41598-023-40688-3 [doi]
PST - epublish
SO  - Sci Rep. 2023 Aug 21;13(1):13584. doi: 10.1038/s41598-023-40688-3.