Abstract
Objectives
To establish an efficient expression system for a fusion protein of glutathione S-transferase and cecropin B (GST-CB) and to clarify the antibacterial mechanism of CB.
Results
The optimal incubation time and methanol concentration for induced expression of CB were 36 h and 1 % w/v, respectively. The yield of GST-CB was 2.2 g/l. The minimum inhibitory concentrations of GST-CB towards Staphylococcus aureus subsp. saprophyticus (ATCC 15305) and Escherichia coli strain CFT073 were 250 and 125 μg/ml, respectively. Notably, mutations of proline 24 (P24) in CB produced a polypeptide without antimicrobial activity.
Conclusion
The fusion protein GST-CB, which has a broad spectrum antimicrobial activity, can be abundantly expressed in Pichia pastoris GS115, and P24 may be an important amino acid for the antimicrobial activity of GST-CB.
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Acknowledgments
This work was supported by Innovation Team Project of the Ministry of Education of China (IRT0959-208).
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Yu, W., Gao, X.J., Liu, Y. et al. Fusion expression of cecropin B-like antibacterial peptide in Pichia GS115 and its antibacterial mechanism. Biotechnol Lett 38, 305–312 (2016). https://doi.org/10.1007/s10529-015-1978-y
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DOI: https://doi.org/10.1007/s10529-015-1978-y