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Heat shock protein: a double-edged sword linking innate immunity and hepatitis B virus infection

Heat shock proteins (HSPs), which have a variety of functions, are one of the stress protein families. In recent years, They have been reported to play a dual role in hepatitis B virus (HBV) which as persistent infection which is associated with, cirrhosis and liver cancer. In this article, we have...

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Autores principales: Dai, Wen-ying, Yao, Guo-qing, Deng, Xi-chuan, Zang, Guang-chao, Liu, Jia, Zhang, Guang-yuan, Chen, Yu-meng, Lv, Ming-qi, Chen, Ting-ting
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10148040/
https://www.ncbi.nlm.nih.gov/pubmed/37128472
http://dx.doi.org/10.1016/j.jve.2023.100322
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author Dai, Wen-ying
Yao, Guo-qing
Deng, Xi-chuan
Zang, Guang-chao
Liu, Jia
Zhang, Guang-yuan
Chen, Yu-meng
Lv, Ming-qi
Chen, Ting-ting
author_facet Dai, Wen-ying
Yao, Guo-qing
Deng, Xi-chuan
Zang, Guang-chao
Liu, Jia
Zhang, Guang-yuan
Chen, Yu-meng
Lv, Ming-qi
Chen, Ting-ting
author_sort Dai, Wen-ying
collection PubMed
description Heat shock proteins (HSPs), which have a variety of functions, are one of the stress protein families. In recent years, They have been reported to play a dual role in hepatitis B virus (HBV) which as persistent infection which is associated with, cirrhosis and liver cancer. In this article, we have summarized the regulatory mechanisms between HSPs and viruses, especially HBV and associated diseases based on HSP biological functions of in response to viral infections. In view of their potential as broad-spectrum antiviral targets, we have also discuss current progress and challenges in drug development based on HSPs, as well as the potential applications of agents that have been evaluated clinically in HBV treatment.
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spelling pubmed-101480402023-04-30 Heat shock protein: a double-edged sword linking innate immunity and hepatitis B virus infection Dai, Wen-ying Yao, Guo-qing Deng, Xi-chuan Zang, Guang-chao Liu, Jia Zhang, Guang-yuan Chen, Yu-meng Lv, Ming-qi Chen, Ting-ting J Virus Erad Review Heat shock proteins (HSPs), which have a variety of functions, are one of the stress protein families. In recent years, They have been reported to play a dual role in hepatitis B virus (HBV) which as persistent infection which is associated with, cirrhosis and liver cancer. In this article, we have summarized the regulatory mechanisms between HSPs and viruses, especially HBV and associated diseases based on HSP biological functions of in response to viral infections. In view of their potential as broad-spectrum antiviral targets, we have also discuss current progress and challenges in drug development based on HSPs, as well as the potential applications of agents that have been evaluated clinically in HBV treatment. Elsevier 2023-03-14 /pmc/articles/PMC10148040/ /pubmed/37128472 http://dx.doi.org/10.1016/j.jve.2023.100322 Text en © 2023 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Review
Dai, Wen-ying
Yao, Guo-qing
Deng, Xi-chuan
Zang, Guang-chao
Liu, Jia
Zhang, Guang-yuan
Chen, Yu-meng
Lv, Ming-qi
Chen, Ting-ting
Heat shock protein: a double-edged sword linking innate immunity and hepatitis B virus infection
title Heat shock protein: a double-edged sword linking innate immunity and hepatitis B virus infection
title_full Heat shock protein: a double-edged sword linking innate immunity and hepatitis B virus infection
title_fullStr Heat shock protein: a double-edged sword linking innate immunity and hepatitis B virus infection
title_full_unstemmed Heat shock protein: a double-edged sword linking innate immunity and hepatitis B virus infection
title_short Heat shock protein: a double-edged sword linking innate immunity and hepatitis B virus infection
title_sort heat shock protein: a double-edged sword linking innate immunity and hepatitis b virus infection
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10148040/
https://www.ncbi.nlm.nih.gov/pubmed/37128472
http://dx.doi.org/10.1016/j.jve.2023.100322
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