Abstract
In this study, we investigated the role of heat shock protein 70 (HSP70) in porcine epidemic diarrhoea virus (PEDV) replication. We found that PEDV infection induced strong HSP70 overexpression in the very early stage of infection. We also confirmed that HSP70 overexpression increased the speed of PEDV replication, resulting in the generation of more virions. In contrast, knockout of HSP70 in cells significantly downregulated PEDV protein expression, resulting in a significant reduction in PEDV replication. Most importantly, we confirmed that among the structural proteins of PEDV, membrane (M) proteins have this important role. We found that membrane proteins control cellular HSP70 expression in PEDV-infected cells. We confirmed HSP70/M complex formation by both immunoprecipitation and immunofluorescence assays. Additionally, PEDV M overexpression induced strong HSP70 expression. All our results clearly confirmed that in PEDV-infected cells, the M protein plays a very important role in PEDV replication in collaboration with HSP70.
Highlights
Viral replication is dependent on host cellular factors [1], several of which are necessary for viral replication [2]
porcine epidemic diarrhoea virus (PEDV) infection significantly increased Heat shock protein 70 (HSP70) expression We investigated the correlation between PEDV infection and HSP70 expression
We found that HSP70 expression was induced at 12 h post-infection, and its levels increased ~tenfold compared to the levels at 8 hpi
Summary
Viral replication is dependent on host cellular factors [1], several of which are necessary for viral replication [2]. In virus-infected cells, proteotoxic stress is strongly induced by viral protein synthesis [3], which has a negative effect on viral replication [4]. Cells respond to stress through adaptive changes that either limit or repair damage, thereby preventing cell death [5]. Heat shock protein 70 (HSP70) is an important protein that promotes cellular homeostasis during metabolism [6]. HSP70, a member of the heat shock protein family, is involved in various cellular processes through its role as a molecular chaperone [7]. It helps refold proteins that are misfolded or aggregated due to cell stress [8].
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