Abstract:The expression levels of proteins in Escherichia coli appear to be preferential for some special codons. In order to enhance the expression level, we designed a partial sequence of the WSSV-VP37 gene based on the codons of E. coli so that its expression level would be optimized. The optimized VP37 fragment was ligated to the expression vector pBAD/gIIIA. Then the resulted recombinant pBAD/gIIIA-VP37p′ was transformed into E. coli Top10 and the cells were induced by L-arabinose. SDS-PAGE analysis showed that the content of VP37p′ constituted 40.5% of the total proteins. Compared with the wild type recombinant pBAD/gIIIA-VP37p, the expression level of the optimized recombinant VP37p′ (40.5% of the total proteins) was significantly higher than that of the wild type VP37p (6.5% of the total proteins).
