Fusion expression of human beta-defensin-2 from multiple joined genes in Escherichia coli.
Human beta-defensin-2 (hBD-2) is a cysteine-rich cationic low molecular weight antimicrobial peptide, which exhibits a broad range of antimicrobial activity without observed acquired resistance. In this work, multiple copies of the hBD-2 gene were linked in tandem and the expression of the multiple joined genes in two fusion expression system, pET28a(+) and pGEX-4T-2, was examined. Using plasmid pET28a(+) with one, two, and four copies of the hBD-2 gene, the expressed level was relatively low, whereas much higher with plasmid pGEX-4T-2, and the fusion products, most of which in insoluble form, account for approximately 26% of the total insoluble cellular proteins.
Wang
Fang
F
Department of Chemical Engineering and Bioengineering, Institute of Bioengineering, Zhejiang University, Hangzhou, P.R. China.
Fang
Xiangming
X
Xu
Zhinan
Z
Peng
Li
L
Cen
Peilin
P
D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D018628:Gene Dosage; D015870:Gene Expression; D006801:Humans; D010957:Plasmids / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000235:genetics; D023083:beta-Defensins / Q000096:biosynthesis* / Q000235:genetics
C106641:DEFB4A protein, human; D011994:Recombinant Proteins; D023083:beta-Defensins