Fusion Expression of Human Beta‐Defensin‐2 from Multiple Joined Genes in Escherichia coli

Abstract

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.

Keywords:

• Antimicrobial peptide
• Expression
• Fusion protein
• Human beta‐defensin‐2
• Tandem genes

Acknowledgments

This work was financially supported by National Natural Science Foundation of China (No. A30070854 & No. 20276066) and the Department of Science and Technology (No. 413491030J30007001103241), Zhejiang Provincial People's Government, People's Republic of China.