The expression of HSP90a has been reported to play an important role in the replication of some viruses, such as Ebola virus, hepatitis C virus, influenza virus, and Japanese encephalitis virus. On the other hand, the reduction of HSP90b has been reported to decrease the correct assembly of human enterovirus 71 viral particles. In this study, HSP90a and heat shock 90kD protein 1, beta were significantly downregulated at 64 hpi in the TGEV-infected ST cells, but were unchanged at 48 hpi,Chlormezanone indicating that they may play a similar role in TGEV infection. Interestingly, a member of the HSP70 protein family, heat shock 70 kDa protein 1B, as well as mitochondrial 60 kDa heat shock protein were both upregulated in infected ST cells at 48 and/or 64 hpi. HSP60 is a mitochondrial chaperonin protein involved in protein folding and a number of extracellular immunomodulatory activities. Elevated expression of HSP60 is associated with a number of inflammatory disorders. HSP70 plays an important role in multiple processes within cells, including protein translation, folding, intracellular trafficking,CAY10505 and degradation. A previous study has revealed that HSP70 is involved in all steps of the viral life cycle, including replication, and is highly specific in regards to viral response, differing from one cell to another for any given virus type. For example, silencing HSP70 expression has been associated with an increase in viral protein levels, while an increase in HSP70 has been suspected to be the initial cellular response to protect against viral infection in rotavirus-infected cells. Further, a recent study showed that HSP70 is an essential host factor for the replication of PRRSV as the silence of HSP70 significantly reduced PRRSV replication. Our results provide new experimental evidence relating the expression of HSP90, HSP70, and HSP60 to TGEV infection, and we speculate that these proteins play a potential role in TGEV replication. Additional work is required to investigate the detailed role of these proteins during TGEV infection. Furthermore, another significantly enriched GO process we observed that 11 significantly altered proteins was immune system processes. Most of these proteins were significantly upregulated at 64 hpi in response to the viral infection, while some were first upregulated at 48 hpi, including CCL5 and TGF-b1. A recent study showed that coronavirus infection of transgenic mice expressing CCL2 led to a dysregulated immune response without effective virus clearance and enhanced death.