Turnover of hepatitis B virus X protein is facilitated by Hdj1, a human Hsp40/DnaJ protein

Sook Young Sohn, Jung Hwan Kim, Kyung Won Baek, Wang Shick Ryu, Byung-Yoon Ahn

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Hepatitis B virus X (HBX) protein is required for the productive infection of hepatitis B virus (HBV) in vivo and implicated in the development of hepatocellular carcinoma. We have previously shown that hTid-1 and Hdj1, the human Hsp40/DnaJ chaperone proteins, bind the HBV core protein and inhibit viral replication in cell culture system. Here, we report evidences to suggest that HBX is the major target of Hdj1 in the inhibition of HBV replication. Expression of Hdj1 in cultured human hepatoma HepG2 cells facilitated degradation of HBX by the proteasome pathway, and thereby inhibited replication of the wild-type HBV as well as that of the HBX-deficient mutant virus rescued by HBX supplied in trans. Mutational analyses indicated that J domain of Hdj1 is required for the process. These results might provide a molecular basis for the antiviral effect of cellular chaperones.

Original languageEnglish
Pages (from-to)764-768
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume347
Issue number3
DOIs
Publication statusPublished - 2006 Sep 1

Fingerprint

HSP40 Heat-Shock Proteins
Viruses
Hepatitis B virus
Hepatocellular Carcinoma
Viral Core Proteins
hepatitis B virus X protein
human DNAJB1 protein
Hep G2 Cells
Proteasome Endopeptidase Complex
Virus Replication
Cell culture
Antiviral Agents
Cell Culture Techniques
Degradation

Keywords

  • Hdj1
  • Hepatitis B virus
  • Hsp40
  • J domain
  • Proteasome
  • X

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Turnover of hepatitis B virus X protein is facilitated by Hdj1, a human Hsp40/DnaJ protein. / Sohn, Sook Young; Kim, Jung Hwan; Baek, Kyung Won; Ryu, Wang Shick; Ahn, Byung-Yoon.

In: Biochemical and Biophysical Research Communications, Vol. 347, No. 3, 01.09.2006, p. 764-768.

Research output: Contribution to journalArticle

Sohn, Sook Young ; Kim, Jung Hwan ; Baek, Kyung Won ; Ryu, Wang Shick ; Ahn, Byung-Yoon. / Turnover of hepatitis B virus X protein is facilitated by Hdj1, a human Hsp40/DnaJ protein. In: Biochemical and Biophysical Research Communications. 2006 ; Vol. 347, No. 3. pp. 764-768.
@article{3be08c171e324ec8a6311848d9f6c08f,
title = "Turnover of hepatitis B virus X protein is facilitated by Hdj1, a human Hsp40/DnaJ protein",
abstract = "Hepatitis B virus X (HBX) protein is required for the productive infection of hepatitis B virus (HBV) in vivo and implicated in the development of hepatocellular carcinoma. We have previously shown that hTid-1 and Hdj1, the human Hsp40/DnaJ chaperone proteins, bind the HBV core protein and inhibit viral replication in cell culture system. Here, we report evidences to suggest that HBX is the major target of Hdj1 in the inhibition of HBV replication. Expression of Hdj1 in cultured human hepatoma HepG2 cells facilitated degradation of HBX by the proteasome pathway, and thereby inhibited replication of the wild-type HBV as well as that of the HBX-deficient mutant virus rescued by HBX supplied in trans. Mutational analyses indicated that J domain of Hdj1 is required for the process. These results might provide a molecular basis for the antiviral effect of cellular chaperones.",
keywords = "Hdj1, Hepatitis B virus, Hsp40, J domain, Proteasome, X",
author = "Sohn, {Sook Young} and Kim, {Jung Hwan} and Baek, {Kyung Won} and Ryu, {Wang Shick} and Byung-Yoon Ahn",
year = "2006",
month = "9",
day = "1",
doi = "10.1016/j.bbrc.2006.06.158",
language = "English",
volume = "347",
pages = "764--768",
journal = "The BMJ",
issn = "0730-6512",
publisher = "Kluwer Academic Publishers",
number = "3",

}

TY - JOUR

T1 - Turnover of hepatitis B virus X protein is facilitated by Hdj1, a human Hsp40/DnaJ protein

AU - Sohn, Sook Young

AU - Kim, Jung Hwan

AU - Baek, Kyung Won

AU - Ryu, Wang Shick

AU - Ahn, Byung-Yoon

PY - 2006/9/1

Y1 - 2006/9/1

N2 - Hepatitis B virus X (HBX) protein is required for the productive infection of hepatitis B virus (HBV) in vivo and implicated in the development of hepatocellular carcinoma. We have previously shown that hTid-1 and Hdj1, the human Hsp40/DnaJ chaperone proteins, bind the HBV core protein and inhibit viral replication in cell culture system. Here, we report evidences to suggest that HBX is the major target of Hdj1 in the inhibition of HBV replication. Expression of Hdj1 in cultured human hepatoma HepG2 cells facilitated degradation of HBX by the proteasome pathway, and thereby inhibited replication of the wild-type HBV as well as that of the HBX-deficient mutant virus rescued by HBX supplied in trans. Mutational analyses indicated that J domain of Hdj1 is required for the process. These results might provide a molecular basis for the antiviral effect of cellular chaperones.

AB - Hepatitis B virus X (HBX) protein is required for the productive infection of hepatitis B virus (HBV) in vivo and implicated in the development of hepatocellular carcinoma. We have previously shown that hTid-1 and Hdj1, the human Hsp40/DnaJ chaperone proteins, bind the HBV core protein and inhibit viral replication in cell culture system. Here, we report evidences to suggest that HBX is the major target of Hdj1 in the inhibition of HBV replication. Expression of Hdj1 in cultured human hepatoma HepG2 cells facilitated degradation of HBX by the proteasome pathway, and thereby inhibited replication of the wild-type HBV as well as that of the HBX-deficient mutant virus rescued by HBX supplied in trans. Mutational analyses indicated that J domain of Hdj1 is required for the process. These results might provide a molecular basis for the antiviral effect of cellular chaperones.

KW - Hdj1

KW - Hepatitis B virus

KW - Hsp40

KW - J domain

KW - Proteasome

KW - X

UR - http://www.scopus.com/inward/record.url?scp=33746368686&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33746368686&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2006.06.158

DO - 10.1016/j.bbrc.2006.06.158

M3 - Article

VL - 347

SP - 764

EP - 768

JO - The BMJ

JF - The BMJ

SN - 0730-6512

IS - 3

ER -