抄録
The glycoprotein E2 sequences of classical swine fever virus (strain p97) were cloned, sequenced and expressed in E. coli. Result from SDS-polyacrylamide gel electrophoresis analysis of expressed proteins revealed the presence of a prominently stained band corresponding to a molecular mass of 61 kDa, which is in agreement with the predicted size from the DNA sequence. The recombinant E2 protein contained an aminoterminal tag of six histidines that could be used for purification by the nickel chelate affinity chromatography. The elution fractions of the expressed protein also contain additional bands of 40 and 35 kDa proteins, indicating proteolytic cleavages might occur. Our Western blotting result also supported that the expression of the recombinant E2 protein of the classical swine fever virus were accomplished.
