Next Article in Journal
Comparative Effectiveness of Different Phase Change Materials to Improve Cooling Performance of Heat Sinks for Electronic Devices
Previous Article in Journal
Transient Changes of Optical Properties in Semiconductors in Response to Femtosecond Laser Pulses
Article Menu

Export Article

Open AccessArticle
Appl. Sci. 2016, 6(9), 240; doi:10.3390/app6090240

Expression, Purification and Antibacterial Activity of NK-Lysin Mature Peptides from the Channel Catfish (Ictalurus punctatus)

1
College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang District Huimin Road No. 211, Chengdu 611130, Sichuan, China
2
Key Laboratory of Animal Disease and Human Health of Sichuan Province, Department of Basic Veterinary Medicine, Sichuan Agricultural University, Wenjiang District Huimin Road No. 211, Chengdu 611130, Sichuan, China
3
Department of Aquaculture, Sichuan Agricultural University, Wenjiang District Huimin Road No. 211, Chengdu 611130, Sichuan, China
*
Author to whom correspondence should be addressed.
Academic Editor: Chih-Ching Huang
Received: 23 June 2016 / Revised: 15 August 2016 / Accepted: 16 August 2016 / Published: 26 August 2016
View Full-Text   |   Download PDF [2150 KB, uploaded 26 August 2016]   |  

Abstract

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. View Full-Text
Keywords: NK-lysins; expression; purification; channel catfish; antibacterial activity NK-lysins; expression; purification; channel catfish; antibacterial activity
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Cai, S.; Wang, J.; Wang, K.; Chen, D.; Dong, X.; Liu, T.; Zeng, Y.; Wang, X.; Wu, D. Expression, Purification and Antibacterial Activity of NK-Lysin Mature Peptides from the Channel Catfish (Ictalurus punctatus). Appl. Sci. 2016, 6, 240.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Appl. Sci. EISSN 2076-3417 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top