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Abstract
Heat shock proteins (HSPs) are a large group of chaperones found in most eukaryotes and bacteria. They are responsible for the correct protein folding, protection of the cell against stressors, presenting immune and inflammatory cytokines; furthermore, they are important factors in regulating cell differentiation, survival and death. Although the biological function of HSPs is to maintain cell homeostasis, some of them can be used by viruses both to fold their proteins and increase the chances of survival in unfavorable host conditions. Folding viral proteins as well as replicating many different viruses are carried out by, among others, proteins from the HSP70 and HSP90 families. In some cases, the HSP70 family proteins directly interact with viral polymerase to enhance viral replication or they can facilitate the formation of a viral replication complex and/or maintain the stability of complex proteins. It is known that HSP90 is important for the expression of viral genes at both the transcriptional and the translational levels. Both of these HSPs can form a complex with HSP90 and, consequently, facilitate the entry of the virus into the cell. Current studies have shown the biological significance of HSPs in the course of infection SARS-CoV-2. A comprehensive understanding of chaperone use during viral infection will provide new insight into viral replication mechanisms and therapeutic potential. The aim of this study is to describe the molecular basis of HSP70 and HSP90 participation in some viral infections and the potential use of these proteins in antiviral therapy.
Highlights
The discovery of Heat Shock Proteins (HSPs) is attributed to the Italian geneticist Ferruccio Ritossa [1], who during his research mistakenly increased the incubation temperature of Drosophila melanogaster larvae, which resulted in an increased transcription of genes of proteins unknown at that time
Such a wide spectrum of activity of HSP70s proves that these proteins, in order to adapt to the conditions of growth and stress in the cell, are able to act on a variety of substrates [11]
The findings suggest that HSP70 and HSP90 are necessary for Dengue Virus (DENV) entry into the cell, and that heat shock stress is optimal for cell replication in the U937 cell line [110]
Summary
The discovery of Heat Shock Proteins (HSPs) is attributed to the Italian geneticist Ferruccio Ritossa [1], who during his research mistakenly increased the incubation temperature of Drosophila melanogaster larvae, which resulted in an increased transcription of genes of proteins unknown at that time. The allosteric mechanism of HSP70 can be modified by J domain proteins (JDP) and nucleotide exchange factors (NEF) [14] Such a wide spectrum of activity of HSP70s proves that these proteins, in order to adapt to the conditions of growth and stress in the cell, are able to act on a variety of substrates [11]. NTD contains in its structure an ATP binding site that is essential for the ATPase activity of HSP90 It is required for the chaperone cycle and protein binding of the HSP90 client [32,33]. HSF1 is the major regulator of HSP90 levels in cells This large influence of HSF1 on HSP90 resulted in the development of a complex series of regulatory mechanisms, including transcription, HSF1 trimerizations, cooperative binding to HSE, post-translational modifications and the ability of HSF1 to directly detect stress. The following subsection focuses on viruses in which both HSP70 and HSP90 are involved
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