Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2023 Mar 14;9(1):100322.
doi: 10.1016/j.jve.2023.100322. eCollection 2023 Mar.

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

Affiliations
Review

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

Wen-Ying Dai et al. J Virus Erad. .

Abstract

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.

Keywords: Antiviral; HSPs; Hepatitis B virus; Molecular chaperones; Vaccine adjuvant.

PubMed Disclaimer

Conflict of interest statement

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Figures

Fig. 1
Fig. 1
HSPs are involved in acquired immunity, monokines and maturation of dendritic cells (DCs), and provide peptides for MHC-loading and antigen-specific responses.
Fig. 2
Fig. 2
Hsp90 interacts with reactive oxygen species (ROS) to promote hepatitis B (HBV) viral capsid assembly, suppresses replication upon glutathione (GSH), and promotes replication after GSH inhibition.
Fig. 3
Fig. 3
Overexpression of Hsp70 promotes both hepatitis B (HBV) replication and suppression.
Fig. 4
Fig. 4
Hsp60 impacts on hepatitis B (HBV) replication and hepatocyte apoptosis by its interaction with HBV pol and HBV virus X protein (HBx).
Fig. 5
Fig. 5
Role of the heat shock protein (HSP) family in hepatitis B (HBV) infection and immune clearance mechanisms.

Similar articles

Cited by

References

    1. Stahl M., Retzlaff M., Nassal M., Beck J. Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system. Nucleic Acids Res. 2007;35(18):6124–6136. - PMC - PubMed
    1. Huang Y-y. Hubei University Of Technology; 2016. Study on Anti-HBV Drugs Targeting Heat Shock Protein.
    1. Yang Y.-X., Huang J.-P., Li S.-N., Li J., Ling T., Xie T., Xu L.-G. HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I. Mol Immunol. 2021;134:62–71. - PubMed
    1. Zhang W.J., Wang R.Q., Li L.T., Fu W., Chen H.C., Liu Z.F. Hsp90 is involved in pseudorabies virus virion assembly via stabilizing major capsid protein VP5. Virology. 2021;553:70–80. - PubMed
    1. Wang X-h, Xu W-h, Zhang X-l, Ma D-y, Lei Y-f, Zheng L., Guo D-x, Wu Z-j, Zhang H., Cao H-w. Effect of PEDV protein on expression of GRP78, the key protein of UPR response in host cells. J Heilongjiang Bayi Agric Univ. 2021;33(4):60–66.

LinkOut - more resources