Both HSP100 and HSP110 have chaperone activity with HSP70, and they can regulate protein aggregation by forming HSP104-HSP70-HSP40 ( 13) and HSP110-HSP70-HSP40 ( 14) ternary complexes to maintain cellular homeostasis in a variety of cellular life activities. Large HSPs, such as HSP100 and HSP110, contain a loop structure that gives them a high capacity of binding to polypeptide substrates or non-protein ligands such as pathogen-associated molecules ( 12). The heat shock protein family is also involved in many fundamental cellular processes including cell cycle control, cell survival, hormone signaling and response to cellular stress through the extensive regulation of intracellular proteins ( 6– 11). They are extensively involved in the lifecycle of proteins, including protein folding and refolding, transport, degradation, assembly, activity regulation, and translocation, as well as the depolymerization of protein aggregates. HSP40, HSP60, HSP70 and HSP90 are well-studied heat shock proteins that often perform biological functions in cells as complexes. Depending on the status of client proteins, sHSPs exert different molecular chaperone functions ( 3– 5). The ability to prevent the aggregation of proteins and polypeptides is the most important function of many sHSPs ( 2). The sHSPs, most of which are heat-inducible, have a wide range of molecular weights from 12-43 kDa and are widely distributed in a variety of tissues. HSPs have a wide range of molecular weights from approximately 10 to 100 kDa and can be classified into different groups according to their molecular weight, including small heat shock proteins (sHSPs), HSP40, HSP60, HSP70, HSP90 and large heat shock proteins ( 1). Heat shock proteins (HSPs) were first discovered in the salivary glands of flies, where they are expressed under heat shock conditions. In this review, we summarize the roles of the heat shock protein family in various stages of viral infection and the potential uses of these proteins in antiviral therapy. However, although the biological function of HSPs is to maintain the homeostasis of cells, some HSPs will also be hijacked by viruses to help their invasion, replication, and maturation, thereby increasing the chances of viral survival in unfavorable conditions inside the host cell. During viral infection, some HSPs can have an antiviral effect by inhibiting viral proliferation through interaction and activating immune pathways to protect the host cell. HSPs protect other proteins under environmental and cellular stress by regulating protein folding and supporting the correctly folded structure of proteins as chaperones. Heat shock proteins (HSPs) are a kind of proteins which mostly found in bacterial, plant and animal cells, in which they are involved in the monitoring and regulation of cellular life activities. 2Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine, Hangzhou, China.1Institute of Biochemistry, College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou, China.
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