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Soluble expression and purification of the anthrax protective antigen in E. coli and identification of a novel dominant-negative mutant N435C.

Appl Microbiol Biotechnol.. 2010-06;  87(2):609-616
Wu G, Feng C, Hong Y, Guo A, Cao S, Dong J, Lin L, Liu Z. State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, People's Republic of China.
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摘要

The anthrax toxin is an AB-type bacterium toxin composed of the protective antigen (PA) as the cell-binding B component, and the lethal factor (LF) and edema toxin (EF) as the catalytic A components. The PA component is a key factor in anthrax-related research and recombinant PA can be produced in general in Escherichia coli. However, such recombinant PA always forms inclusion bodies in the cytoplasm of E. coli, making difficult the procedure of its purification. In this study, we found that the solubility of recombinant PA was dramatically enhanced by fusion with glutathione S-transferase (GST) and an induction of its expression at 28 degrees C. The PA was purified to high homogeneity and a yield of 3 mg prote... More

关键词

Bacillus anthracis; Protective antigen; Soluble expression; Dominant-negative mutant
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