Codon optimization

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.

Effect of codon optimization on expression levels of human cystatin C in Pichia pastoris

Y. M. Li, Li, D. J., Xu, X. J., Cui, M., Zhen, H. H., and Wang, Q., Effect of codon optimization on expression levels of human cystatin C in Pichia pastoris, vol. 13, pp. 4990-5000, 2014.

Human cystatin C (CysC) is a cysteine proteinase inhibitor with many potential applications. To facilitate further studies of the functions and applications of CysC, we improved the heterologous expression of CysC using a basic codon optimization method. In this study, we cloned the high-GC content wild-type sequence of the CysC gene and also designed a slightly AT-biased sequence, with codons optimized for expression in the Pichia pastoris GS115 strain.

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