Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo.
作者信息
Cho Dae-Yeon, Yang Gi-Hyeok, Ryu Chun Jeih, Hong Hyo Jeong
机构信息
Antibody Engineering Research Unit, Laboratory of Immunology, Korea Research Institute of Bioscience and Biotechnology, Yusong, Taejon 305-600, Korea.
出版信息
J Virol. 2003 Feb;77(4):2784-8. doi: 10.1128/jvi.77.4.2784-2788.2003.
Abstract
The proper folding and assembly of viral envelope proteins are mediated by host chaperones. In this study, we demonstrated that an endoplasmic reticulum luminal chaperone GRP78/BiP bound specifically to the pre-S1 domain of the L protein in vitro and in vivo where complete viral particles were secreted, suggesting that GRP78/BiP plays an essential role in the proper folding of the L protein and/or assembly of viral envelope proteins.
摘要
相似文献
1
Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo.
J Virol. 2003 Feb;77(4):2784-8. doi: 10.1128/jvi.77.4.2784-2788.2003.
2
Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein.
FEBS Lett. 2008 Sep 22;582(21-22):3179-84. doi: 10.1016/j.febslet.2008.07.062. Epub 2008 Aug 15.
3
Chaperones involved in hepatitis B virus morphogenesis.
Biol Chem. 1999 Mar;380(3):305-14. doi: 10.1515/BC.1999.042.
4
5
Activation of the grp78 and grp94 promoters by hepatitis C virus E2 envelope protein.
J Virol. 1999 May;73(5):3718-22. doi: 10.1128/JVI.73.5.3718-3722.1999.
6
ADP-ribosylation of the molecular chaperone GRP78/BiP.
Mol Cell Biochem. 1994 Sep;138(1-2):141-8. doi: 10.1007/BF00928456.
7
Involvement of the molecular chaperone BiP in maturation of Sindbis virus envelope glycoproteins.
J Virol. 1995 Mar;69(3):1621-7. doi: 10.1128/JVI.69.3.1621-1627.1995.
8
Flux of the paramyxovirus hemagglutinin-neuraminidase glycoprotein through the endoplasmic reticulum activates transcription of the GRP78-BiP gene.
J Virol. 1991 Jul;65(7):3590-7. doi: 10.1128/JVI.65.7.3590-3597.1991.
9
Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene.
Mol Biol Cell. 1992 Feb;3(2):143-55. doi: 10.1091/mbc.3.2.143.
10
Enhanced binding to the molecular chaperone BiP slows thyroglobulin export from the endoplasmic reticulum.
Mol Endocrinol. 1998 Mar;12(3):458-67. doi: 10.1210/mend.12.3.0069.
引用本文的文献
1
COVID-19, Obesity, and GRP78: Unraveling the Pathological Link.
J Obes Metab Syndr. 2023 Sep 30;32(3):183-196. doi: 10.7570/jomes23053.
2
Release of hepatitis B virions is positively regulated by glucose-regulated protein 78 through direct interaction with preS1.
J Med Virol. 2023 Jan;95(1):e28271. doi: 10.1002/jmv.28271.
3
GRP78, a Novel Host Factor for SARS-CoV-2: The Emerging Roles in COVID-19 Related to Metabolic Risk Factors.
Biomedicines. 2022 Aug 17;10(8):1995. doi: 10.3390/biomedicines10081995.
4
Pathogenicity and virulence of Hepatitis B virus.
Virulence. 2022 Dec;13(1):258-296. doi: 10.1080/21505594.2022.2028483.
5
Possible Involvement of Adipose Tissue in Patients With Older Age, Obesity, and Diabetes With SARS-CoV-2 Infection (COVID-19) via GRP78 (BIP/HSPA5): Significance of Hyperinsulinemia Management in COVID-19.
Diabetes. 2021 Dec;70(12):2745-2755. doi: 10.2337/db20-1094. Epub 2021 Oct 6.
6
Proteomic Discovery of VEEV E2-Host Partner Interactions Identifies GRP78 Inhibitor HA15 as a Potential Therapeutic for Alphavirus Infections.
Pathogens. 2021 Mar 2;10(3):283. doi: 10.3390/pathogens10030283.
7
Hepatocyte Endoplasmic Reticulum Stress Inhibits Hepatitis B Virus Secretion and Delays Intracellular Hepatitis B Virus Clearance After Entecavir Treatment.
Front Med (Lausanne). 2021 Feb 4;7:589040. doi: 10.3389/fmed.2020.589040. eCollection 2020.
8
9
Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development.
Signal Transduct Target Ther. 2020 Jul 13;5(1):125. doi: 10.1038/s41392-020-00233-4.
10
Medicinal chemistry strategies toward host targeting antiviral agents.
Med Res Rev. 2020 Sep;40(5):1519-1557. doi: 10.1002/med.21664. Epub 2020 Feb 14.
本文引用的文献
1
Fine mapping of virus-neutralizing epitopes on hepatitis B virus PreS1.
Virology. 2000 Apr 25;270(1):9-16. doi: 10.1006/viro.2000.0250.
2
An 80-kilodalton protein that binds to the pre-S1 domain of hepatitis B virus.
J Virol. 2000 Jan;74(1):110-6. doi: 10.1128/jvi.74.1.110-116.2000.
3
Chaperones involved in hepatitis B virus morphogenesis.
Biol Chem. 1999 Mar;380(3):305-14. doi: 10.1515/BC.1999.042.
4
Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins.
J Virol. 1998 May;72(5):3851-8. doi: 10.1128/JVI.72.5.3851-3858.1998.
5
Sequence-specific repression of cotranslational translocation of the hepatitis B virus envelope proteins coincides with binding of heat shock protein Hsc70.
Virology. 1997 Aug 18;235(1):144-52. doi: 10.1006/viro.1997.8689.
6
Formation of intracellular particles by hepatitis B virus large surface protein.
J Virol. 1997 Jul;71(7):5487-94. doi: 10.1128/JVI.71.7.5487-5494.1997.
7
In vitro neutralization of hepatitis B virus by monoclonal antibodies against the viral surface antigen.
J Med Virol. 1997 Jun;52(2):226-33. doi: 10.1002/(sici)1096-9071(199706)52:2<226::aid-jmv18>3.0.co;2-i.
8
Folding of rabies virus glycoprotein: epitope acquisition and interaction with endoplasmic reticulum chaperones.
J Virol. 1997 May;71(5):3742-50. doi: 10.1128/JVI.71.5.3742-3750.1997.
9
Hepatitis B virus morphogenesis.
Curr Top Microbiol Immunol. 1996;214:297-337. doi: 10.1007/978-3-642-80145-7_10.
10
ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.
Nature. 1993 Oct 14;365(6447):664-6. doi: 10.1038/365664a0.
Zotero 插件