Expression, Purification and Antibacterial Activity of NK-Lysin Mature Peptides from the Channel Catfish (Ictalurus punctatus)
| Autor: | Jun Wang, Xiaowei Dong, Xingli Wang, Defang Chen, Tao Liu, Shurui Cai, Yu-kun Zeng, Dongmei Wu, Kaiyu Wang |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
purification Antimicrobial peptides Lysin Peptide lcsh:Technology lcsh:Chemistry 03 medical and health sciences 0302 clinical medicine Affinity chromatography antibacterial activity expression General Materials Science Instrumentation lcsh:QH301-705.5 Fluid Flow and Transfer Processes chemistry.chemical_classification biology Chemistry lcsh:T Process Chemistry and Technology General Engineering NK-lysins channel catfish biology.organism_classification Antimicrobial Fusion protein Molecular biology lcsh:QC1-999 Computer Science Applications 030104 developmental biology Biochemistry lcsh:Biology (General) lcsh:QD1-999 lcsh:TA1-2040 Ictalurus lcsh:Engineering (General). Civil engineering (General) lcsh:Physics 030215 immunology Catfish |
| Zdroj: | Applied Sciences; Volume 6; Issue 9; Pages: 240 Applied Sciences, Vol 6, Iss 9, p 240 (2016) |
| ISSN: | 2076-3417 |
| DOI: | 10.3390/app6090240 |
| Popis: | Antimicrobial peptides (AMPs) are small peptides and play important roles in host innate immune response against microbial invasion. Aquatic animals secrete different kinds of antimicrobial peptides which have antimicrobial activity towards microorganisms. NK-lysins, mature peptides produced by cytotoxic T lymphocytes and natural killer cells, are comprised of 74–78 amino acid residues, demonstrating broad-spectrum antimicrobial activity against bacteria, fungi, protozoa, and parasites. In this study, three distinct NK-lysin mature peptide (mNKLs), transcripts (76 amino acid residues) cloned from the channel catfish (Ictalurus punctatus) head kidney were ligated into plasmid vector pET-32a(+) to express the mNKLs fusion protein. The fusion protein was successfully expressed in E. coli Rosetta (DE3) under optimized conditions. After purification by affinity column chromatography, the fusion protein was successfully cleaved by enterokinase and released the peptide mNKLs. Tricine-SDS-PAGE results showed that mNKLs (approximately 8.6 kDa) were successfully expressed. The purified peptide mNKLs exhibited antibacterial activity against Staphylococcus aureus and E. coli. |
| Databáze: | OpenAIRE |
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