Issue |
E3S Web Conf.
Volume 78, 2019
2018 International Seminar on Food Safety and Environmental Engineering (FSEE 2018)
|
|
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Article Number | 02002 | |
Number of page(s) | 6 | |
Section | Food Safety, Extraction and Food Engineering | |
DOI | https://doi.org/10.1051/e3sconf/20197802002 | |
Published online | 15 January 2019 |
Anti-Vibrio Response of CarcininPm 1 from Penaeus monodon and Its Heterologous Expression
1
Guangdong Technology Research Center for Marine Algal Bioengineering, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, PR China
2
South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou, 518121, PR China
Crustins are crucial antimicrobial peptides in shrimp and play very important roles in innate immunity. In this research, a Type I crustin from Penaeus monodon (CarcininPm1) contained 108 residues was studied. The first 16 residues are signal peptide. It contained ten cysteines but did not form an intact whey acidic protein (WAP) domain. CarcininPm1 was observed to widely distribute in all tissues, while highly expressed in intestine. The expression level of CarcininPm1 in hepatopancreas was up-regulated 12- 20 times during 4-12h post challenged by Vibrio parahaemolyticus. And the transcription in heart, stomach and gills was also significantly enhanced at 4h post challenge. The mature peptide was expressed successfully in Eschericha coli by fusing to a SUMO protein, with protein production around 8 mg/mL. After cleavage with SUMO protease, carcininPm1 was obtained indicating its potential applications.
© The Authors, published by EDP Sciences, 2019
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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