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KMID : 0613820220320120956
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Journal of Life Science
2022 Volume.32 No. 12 p.956 ~ p.961
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expression of Antimicrobial Peptide (AMP), Moricin Using SUMO Fusion Tag in Escherichia coli
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Ahn Dong-gyu
Park Sun-Ill
Kim Soon-Young
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Abstract
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Plant Chloroplast have several advantages as an expression platform of biopharmaceuticals over con- ventional expression platforms such as mammalian cells, yeast and bacteria. First, plants do not serve as a host for mammalian infectious virus and have endotoxin like bacteria which can cause anaphylactic shock. In addition, high copy number of chloroplast genome allows for chloroplast transformants to reach the high level of expression of heterologous genes. Moreover, the integration of transgenes into specific region of chloroplast genomes makes chloroplast transformants unaffected by positional effect which can be frequently observed from nuclear transformants, resulting in loss of transgene
expressions. Antimicrobial peptides (AMPs) are a kind of innate immunity which is found from bacteria to humans. Unlike conventional antibiotics, very less dosage of AMPs can have catastrophic effect on bacterial survival. Further, the repeated use of AMPs does not trigger the development of bacterial resistance. Moricin, one of the AMPs, was isolated from Bombyx mori, a silkworm moth. The C-termi- nal of moricin consists largely of basic amino acids, and the N-terminal has an α-helix structure. Moricin was chosen and expressed in a SUMO/SUMOase without leaving any unwanted amino acids which could potentially affect the anti-bacterial activity of the moricin. The transformation vector used in this study has already been created in this lab for the expression in both prokaryotic systems such as E. coli and chloroplast. The expressed moricin was purified using Ni columns and SUMOase, and the antibacterial activity of the purified moricin was confirmed using an agar diffusion assay
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KEYWORD
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Antimicrobial peptide, chloroplast, Escherichia coli, moricin, small ubiquitin-related modifier (SUMO)
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