Abstract
BackgroundSuccessful viral infection requires the involvement of host cellular factors in their life cycle. Heat shock protein 70 (HSP70) can be recruited by numerous viruses to promote the folding, maturation, or assembly of viral proteins. We have previously shown that HSP70 is significantly elevated in porcine reproductive and respiratory syndrome virus (PRRSV)-infected lungs, suggesting HSP70 may play a potential role during PRRSV infection. In this study, we tried to investigate the role of HSP70 during PRRSV infection.ResultsIn this study, we observed that PRRSV infection induced the expression of HSP70. The down-regulation of HSP70 using quercetin, a HSPs synthesis inhibitor, or small interfering RNAs (siRNA) reduced the viral protein level and viral production. Notably, these inhibitory effects on PRRSV infection could be attenuated by heat shock treatment. In addition, HSP70 was found to colocalize with the viral double-stranded RNA (dsRNA) and knockdown of HSP70 decreased the dsRNA levels, suggesting HSP70 is involved in the formation of viral replication and transcription complex (RTC) and thus affects the viral replication.ConclusionsOur study revealed that HSP70 is an essential host factor required for the replication of PRRSV. The inhibition of HSP70 significantly reduced PRRSV replication, which may be applied as an effective antiviral strategy.
Highlights
Successful viral infection requires the involvement of host cellular factors in their life cycle
We have previously shown that transcript abundance of Heat shock protein 70 (HSP70) is elevated in porcine reproductive and respiratory syndrome virus (PRRSV) infected lungs relative to uninfected negative control (UNC) lungs [27], suggesting HSP70 may play a potential role in PRRSV infection
PRRSV infection induces the expression of HSP70 We firstly investigated the effect of PRRSV infection on the expression of HSP70
Summary
Successful viral infection requires the involvement of host cellular factors in their life cycle. Porcine reproductive and respiratory syndrome (PRRS) is considered to be one of the most significant viral diseases, causing serious economic losses to the swine industry worldwide [1]. The nonstructural proteins (NSPs) are encoded in ORF1a and ORF1b, which are situated in the 5’-proximal two-thirds of the genome. Some of these NSPs and host cellular factors are assembled into the double membrane vesicles (DMVs) derived from endoplasmic reticulum (ER) to form the viral replication and transcription complex (RTC) for viral replication, subgenomic (sg) mRNA transcription, and translation [4,5].
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