This analysis indicated that six biological processes were significantly affected at 48 and 64 hpi, and the differentially expressed proteins involved in these processes were almost the same. The large overlap between the two time points suggests that some of the same sets of host proteins or processes were disturbed at these times. However, it is also likely that some processes were affected solely at one time point or the other. At 48 hpi, Diphenhydramine hydrochloride serine/threonineprotein phosphatase PP1-beta-catalytic subunit, scavenger receptor class B member 1, transforming growth factor-beta-induced protein ig-h3, and predicted inositol 1,4,5-trisphosphate receptor type 3 were uniquely altered, likely indicating changes in cell adhesion and/or cell-cell signaling processes. At 64 hpi, on the other hand, calreticulin, predicted tumor- associated calcium signal transducer 2-like, vascular cell adhesion molecule, galectin-3, glutamate dehydrogenase 1, and C–X-C motif chemokine 16 were uniquely changed, also indicating changes in cell adhesion and/or Trifluridine cell-cell signaling as well as extracellular matrix organization and locomotion. We believe that these uniquely altered proteins reflect changes in specific/specialized processes at each time point that are tightly linked to the temporal changes observed in the host cell morphology and gene/protein expression after TGEV infection. The most significantly enriched GO category related to the differentially expressed proteins was stress, which included 12 differentially expressed proteins at 48 hpi and 27 different proteins at 64 hpi. The increased number of proteins association with this GO term at 48 hpi likely highlights the initial upregulation of the cellular stress response, while the higher number at 64 hpi indicates that the stress response to TGEV infection is likely more fully induced at this later stage. HSPs, also known as stress proteins, are often involved in the cellular response to stress, influencing changes in the state or activity of the cell or organism. HSP90, which has two isoforms, is one of the most abundant molecular chaperones that is induced in response to cellular stress, and it functions to stabilize proteins involved in cell growth and anti-apoptotic signaling. In additional, TGEV-infection can induce the expression of proinflammatory genes, including CCL2, CCL5, and probable ATP-dependent RNA helicase DDX58, in cell culture and in vivo in the absence of viral protein 7.