Lubkowska Anna, Pluta Waldemar, Strońska Aleksandra, Lalko Alicja
Department of Functional Diagnostics and Physical Medicine, Pomeranian Medical University in Szczecin, Żołnierska 54, 71-210 Szczecin, Poland.
Department of Pharmacognosy and Natural Medicines, Pomeranian Medical University in Szczecin, Powstańców Wlkp. 72, 70-111 Szczecin, Poland.
Int J Mol Sci. 2021 Aug 29;22(17):9366. doi: 10.3390/ijms22179366.
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.
热休克蛋白（HSPs）是在大多数真核生物和细菌中发现的一大类伴侣蛋白。它们负责蛋白质的正确折叠，保护细胞免受应激源影响，呈递免疫和炎性细胞因子；此外，它们是调节细胞分化、存活和死亡的重要因素。尽管热休克蛋白的生物学功能是维持细胞稳态，但其中一些可被病毒利用来折叠其蛋白质并增加在不利宿主条件下的存活几率。热休克蛋白70（HSP70）家族和热休克蛋白90（HSP90）家族的蛋白质等参与了病毒蛋白的折叠以及多种不同病毒的复制。在某些情况下，HSP70家族蛋白直接与病毒聚合酶相互作用以增强病毒复制，或者它们可以促进病毒复制复合体的形成和/或维持复合蛋白的稳定性。已知HSP90在转录和翻译水平上对病毒基因的表达都很重要。这两种热休克蛋白都可以与HSP90形成复合物，从而促进病毒进入细胞。目前的研究已经表明了热休克蛋白在严重急性呼吸综合征冠状病毒2（SARS-CoV-2）感染过程中的生物学意义。全面了解病毒感染期间伴侣蛋白的作用将为病毒复制机制和治疗潜力提供新的见解。本研究的目的是描述HSP70和HSP90参与某些病毒感染的分子基础以及这些蛋白质在抗病毒治疗中的潜在用途。
