Mode of Action of Heat Shock Protein (HSP) Inhibitors against Viruses through Host HSP and Virus Interactions

Shuang Wu; Yongtian Zhao; Delu Wang; Zhuo Chen

doi:10.3390/genes14040792

Mode of Action of Heat Shock Protein (HSP) Inhibitors against Viruses through Host HSP and Virus Interactions

Genes (Basel). 2023 Mar 25;14(4):792. doi: 10.3390/genes14040792.

Authors

Shuang Wu¹, Yongtian Zhao^{1

2}, Delu Wang³, Zhuo Chen¹

Affiliations

¹ Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Guizhou University, Guiyang 550025, China.
² College of Life Science and Agriculture, Qiannan Normal University for Nationalities, Duyun 558000, China.
³ College of Forestry, Guizhou University, Guiyang 550025, China.

Abstract

Misfolded proteins after stress-induced denaturation can regain their functions through correct re-folding with the aid of molecular chaperones. As a molecular chaperone, heat shock proteins (HSPs) can help client proteins fold correctly. During viral infection, HSPs are involved with replication, movement, assembly, disassembly, subcellular localization, and transport of the virus via the formation of macromolecular protein complexes, such as the viral replicase complex. Recent studies have indicated that HSP inhibitors can inhibit viral replication by interfering with the interaction of the virus with the HSP. In this review, we describe the function and classification of HSPs, the transcriptional mechanism of HSPs promoted by heat shock factors (HSFs), discuss the interaction between HSPs and viruses, and the mode of action of HSP inhibitors at two aspects of inhibiting the expression of HSPs and targeting the HSPs, and elaborate their potential use as antiviral agents.

Keywords: HSP inhibitors; antiviral activity; heat shock proteins; interaction; molecular mechanism; virus.

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

Heat-Shock Proteins* / metabolism
Heat-Shock Response
Humans
Molecular Chaperones / metabolism
Viruses*

Substances

Heat-Shock Proteins
Molecular Chaperones

Grants and funding

This work was supported by the National Key Research Development Program of China (2022YFD1700504), the National Natural Science Foundation of China (No. 21977023, No. 31860515), the Post-subsidy project of the National Key Research Development Program of China (2018-5262), the China Agriculture Research System (CARS-23-C07), Program of Introducing Talents to Chinese Universities (D20023), and Major Supported Project of Foreign Experts (110000210820228008).