Heat resistance

Codon optimization enhances the expression of porcine β-defensin-2 in Escherichia coli

C. Y. Gao, Xu, T. T., Zhao, Q. J., and Li, C. L., Codon optimization enhances the expression of porcine β-defensin-2 in Escherichia coli, vol. 14, pp. 4978-4988, 2015.

Porcine β-defensin-2 (pBD2) is a cationic antimicrobial peptide that has therapeutic potential. The amount of pBD2 in nature is limited, and the expression of pBD2 in Escherichia coli is low, probably because a different gene codon is used by prokaryotic organisms to that used by eukaryotes. Codon preference optimization is one of the ways to increase heterologous expression of pBD2. To achieve high expression of pBD2, the pBD2 gene was redesigned according to the preferred codon in E. coli without altering the amino acid sequence.

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