PMC:7281546 / 45909-47211 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7281546","sourcedb":"PMC","sourceid":"7281546","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7281546","text":"Heat shock protein 27 (HSP27) belongs to the small heat shock proteins family, which has been identified as a multifunctional protein involved in cytoskeletal stability, proinflammatory processes, and the inhibition of apoptosis [222,223]. Several HSPs have been reported to be implicated in PEDV infection in vitro and in vivo [224,225]. Indeed, the infection of many viruses up-regulates HSP27 expression by different mechanisms to delay cellular apoptosis, then supplies sufficient time for viral replication [226,227]. However, PEDV infection significantly induces the decreased expression of HSP27 in Vero cells [225] and MARC-145 cells [228]. HSP27 activates the phosphorylation of NF-κB, and thus promotes the mRNA expression of IFN-β in MARC-145 cells. As HSP27 is an upstream regulator of antiviral immune signaling, overexpression of HSP27 significantly inhibits the PEDV replication. PEDV has developed a strategy via mediating the suppression of HSP27 production to escape from host innate immune response [228]. HSP70, the most conserved HSP, is also important for the multiplication of several CoVs. The recruitment of HSP70 is thought to be a viral survival strategy for several viruses in their hosts [229]. The relationship between HSP70 and PEDV should be exploited further in 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