Echovirus is an important cause of
viral pneumonia and
encephalitis in infants, neonates, and young children worldwide. However, the exact mechanism of its pathogenesis is still not well understood. Here, we established an echovirus type 9
infection mice model, and performed two-dimensional gel electrophoresis (2DE) and tandem mass spectrometry (MS/MS)-based comparative proteomics analysis to investigate the differentially expressed host
proteins in mice brain. A total of 21 differentially expressed
proteins were identified by MS/MS. The annotation of the differentially expressed
proteins by function using the UniProt and GO databases identified one
viral protein (5%), seven
cytoskeletal proteins (33%), six macromolecular biosynthesis and metabolism
proteins (28%), two stress response and chaperone
binding proteins (9%), and five other cellular
proteins (25%). The subcellular locations of these
proteins were mainly found in the cytoskeleton, cytoplasm, nucleus, mitochondria, and Golgi apparatus. The
protein expression profiles and the results of quantitative RT-PCR in the detection of gene transcripts were found to
complement each other. The differential protein interaction network was predicted using the STRING database. Of the identified
proteins,
heat shock protein 70 (Hsp70), showing consistent results in the proteomics and transcriptomic analyses, was analyzed through Western blotting to verify the reliability of differential
protein expression data in this study. Further, evaluation of the function of Hsp70 using
siRNA and
quercetin, an inhibitor of Hsp70, showed that Hsp70 was necessary for the
infection of echovirus type 9. This study revealed that
echovirus infection could cause the differential expression of a series of host
proteins, which is helpful to reveal the pathogenesis of
viral infection and identify therapeutic
drug targets. Additionally, our results suggest that Hsp70 could be a useful therapeutic host
protein target for
echovirus infection.