World Aquaculture Society Meetings

facebook

Your browser does not support the most current secure communications protocol. The World Aquaculture Society is committed to the security of your private information. In order to accept credit card data on this site we are recquired to be in compliance with Payment Card Industry (PCI) standards. Current PCI standards will not allow us to accept traffic from browsers that do not support TLS 1.2 after June 30, 2018. We are alerting you to the important need to update your browser. Changes to our web server made on or before June 30, 2018 will make was.org unavailable with the browser you are currently using. [More..]

Add To Calendar 28/04/2016 08:30:0028/04/2016 08:50:00America/Los_AngelesAsian-Pacific Aquaculture 2016PANCREATIC RIBONUCLEASE (RNASE1) WITH DIGESTIVE AND ANTIMICROBIAL FUNCTIONS IN HERBIVOROUS Megalobrama amblycephala   Crystal 3The World Aquaculture Societyjohnc@was.orgfalseanrl65yqlzh3g1q0dme13067DD/MM/YYYY

PANCREATIC RIBONUCLEASE (RNASE1) WITH DIGESTIVE AND ANTIMICROBIAL FUNCTIONS IN HERBIVOROUS Megalobrama amblycephala  

Han Liu*, Yanhe Li, Weimin Wang**
College of Fisheries, Huazhong Agricultural University, Wuhan, 430070, China. E-mail address: lifegood1986@126.com . **Corresponding author.

Pancreatic ribonuclease (RNase1), an important digestive enzyme, has been used as a model protein with which to study the molecular evolutionary and physiological functions of mammals. Here, we identified the RNase1 genes from five fish species and characterized the expression and function of RNase1 in the herbivorous Megalobrama amblycephala. The five identified fish RNase1 genes all have the signature motifs of the RNase A superfamily: CKXXNTF, six conserved cysteines, and the catalytic histidine-lysine-histidine triad. M. amblycephala RNase1 (Ma-RNase1) was weakly expressed in the early developmental stages and strongly expressed in the adult liver and spleen. A biological functional analysis of the recombinant protein demonstrated that Ma-RNase1 had a relatively strong ribonuclease activity at its optimal pH 6.1, which is consistent with the pH of its intestinal microenvironment. Ma-RNase1 also exhibited potent antimicrobial activity against the Gram-negative bacteria Escherichia coli and Gram-positive bacteria Staphylococcus aureus and Bacillus subtilis. These results, together with the presence of ribonuclease activity in mammals RNase1 and bactericidal activity in other teleosts, strongly suggest that Ma-RNase1 has both digestive and antimicrobial activities and that these functions result from its adaptive diversification during the evolution of the species.




Copyright © 2001-2018 World Aquaculture Society All Rights Reserved.