Abstract
Escherichia coli BL21(DE3) was transformed with a pHCD1 plasmid harboring the human β-defensin-1 ( hBD1 ) gene fused in frame behind a disulfide bond isomerase (DsbC), a His-tag, and an enterokinase cleavage site. After induction, the DsbC-hBD1 was expressed as a ~36 kDa soluble fusion protein in recombinant E. coli, which also inhibited host cell growth. After cell disruption, the soluble protein was easily recovered by Ni 2+ affinity chromatography and cleaved by enterokinase to yield a mature hBD1 of about 4 kDa. Importantly, the mature hBD1 showed broad antimicrobial activity against Gram-positive and -negative pathogenic bacteria, including Streptococcus pneumoniae , E. coli O157:H7, and Klebsiella pneumoniae. Key words : Antimicrobial activity, Escherichia coli , human β-defensin-1, soluble expression.
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