Abstract: 【Objective】 The objective of this study is to analyze the protein expression changes of the MARC-145 which was infected with highly pathogenic PRRSV. Proteomic techniques were used to establish the protein expression profiles. The study provides the global information of proteomic alteration of MARC-145 cells in the presence of intact PRRSV and the clues for further understanding of the mechanism of interaction. 【Method】 The differentially expressed proteins between the MARC-145 cells that were infected with highly pathogenic PRRSV and the normal MARC-145 cells were profiled and identified by two dimensional electrophoresis and Western Blotting. Differential proteinaceous information was identified by mass chromatographic analysis and retrieval. 【Result】The results showed that there were seven differentially expressed proteins. Five proteins were identified successfully which were heat-shock 70-kD protein, thioredoxin, S100 calcium-binding protein A6, glyceraldehyde-3-phosphate dehydrogenase, and beta-actin, respectively. Among them, the heat-shock 70-kD protein and S100 calcium-binding protein A6 were down-regulated proteins; thioredoxin, glyceraldehyde-3-phosphate dehydrogenase, and beta-actin were up-regulated proteins. The function of the five proteins were closely associated with the growth, apoptosis, santioxidant and ignal transduction of MARC-145 cells. 【Conclusion】The quantity of functional proteins of the MARC-145 was changed which were infected by highly pathogenic PRRSV.

Key words: porcine productive and respiratory syndrome virus, MARC-145 cells, proteomics