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

doi:10.1016/j.bbrc.2006.06.158

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 journal › Article › peer-review

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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 language	English
Pages (from-to)	764-768
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	347
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2006.06.158
Publication status	Published - 2006 Sept 1

Bibliographical note

Funding Information:
This work was supported by a Grant (2005-015-E00088) from the Korea Research Foundation. S.-Y. Sohn and K.-W. Baek received the BK21 fellowship from the Korean Ministry of Education.

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2006.06.158

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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.",

author = "Sohn, {Sook Young} and Kim, {Jung Hwan} and Baek, {Kyung Won} and Ryu, {Wang Shick} and Ahn, {Byung Yoon}",

note = "Funding Information: This work was supported by a Grant (2005-015-E00088) from the Korea Research Foundation. S.-Y. Sohn and K.-W. Baek received the BK21 fellowship from the Korean Ministry of Education.",

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AU - Sohn, Sook Young

AU - Kim, Jung Hwan

AU - Baek, Kyung Won

AU - Ryu, Wang Shick

AU - Ahn, Byung Yoon

N1 - Funding Information: This work was supported by a Grant (2005-015-E00088) from the Korea Research Foundation. S.-Y. Sohn and K.-W. Baek received the BK21 fellowship from the Korean Ministry of Education.

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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.

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

Abstract

Bibliographical note

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UN SDGs

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