Enhanced cecropin B2 production via chitin‐binding domain and intein self‐cleavage system
| Autor: | Yi-Ting Fang, Jyung-Hurng Liu, Wei-Shiang Lai, Yung-Chuan Liu |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Acinetobacter baumannii
0106 biological sciences Staphylococcus aureus Recombinant Fusion Proteins Biomedical Engineering Bioengineering Peptide medicine.disease_cause 01 natural sciences Applied Microbiology and Biotechnology law.invention 03 medical and health sciences Chitin binding law 010608 biotechnology Drug Discovery Escherichia coli medicine 030304 developmental biology chemistry.chemical_classification 0303 health sciences Process Chemistry and Technology General Medicine Antimicrobial Cecropin Biochemistry chemistry Recombinant DNA Insect Proteins Molecular Medicine Intein Self cleavage Antimicrobial Cationic Peptides Biotechnology |
| Zdroj: | Biotechnology and Applied Biochemistry. 66:209-215 |
| ISSN: | 1470-8744 0885-4513 |
| DOI: | 10.1002/bab.1716 |
| Popis: | In this study, various constructs and hosts were used to produce high levels of cecropin B2 (cecB2). To mitigate cecB2's toxic inhibition of host cells, various cecB2 constructs were built. Results showed that the combination of a chitin-binding domain and an intein self-cleavage motif in front of cecropin B2, without a His-tag, was best for cecB2 expression. E. coli ER2566 was the best host, and 2YT was the best medium for cultivation. Under these conditions, a cecB2 yield of 98.2 mg/L could be obtained after purification. The purified cecB2 expressed a wide antimicrobial effect on most Gram-negative strains, including multidrug-resistant Acinetobactor baumannii and Staphylococcus aureus. This study provides a systematic approach to the efficient production of the antimicrobial peptide (AMP) cecB2 via the recombinant E. coli process, which is expected to be an efficient way for the production of other AMPs. |
| Databáze: | OpenAIRE |
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