Toxins 2017, 9(1), 15; doi:10.3390/toxins9010015
Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom
1
Faculty of Medicine, Chulalongkorn University, Bangkok 10330, Thailand
2
Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, UK
*
Authors to whom correspondence should be addressed.
Academic Editors: Jay Fox and José María Gutiérrez
Received: 23 October 2016 / Revised: 21 December 2016 / Accepted: 23 December 2016 / Published: 30 December 2016
(This article belongs to the Special Issue Snake Venom Metalloproteinases)
Abstract
Russell’s viper bites are potentially fatal from severe bleeding, renal failure and capillary leakage. Snake venom metalloproteinases (SVMPs) are attributed to these effects. In addition to specific antivenom therapy, endogenous inhibitors from snakes are of interest in studies of new treatment modalities for neutralization of the effect of toxins. Two major snake venom metalloproteinases (SVMPs): RVV-X and Daborhagin were purified from Myanmar Russell’s viper venom using a new purification strategy. Using the Next Generation Sequencing (NGS) approach to explore the Myanmar RV venom gland transcriptome, mRNAs of novel tripeptide SVMP inhibitors (SVMPIs) were discovered. Two novel endogenous tripeptides, pERW and pEKW were identified and isolated from the crude venom. Both purified SVMPs showed caseinolytic activity. Additionally, RVV-X displayed specific proteolytic activity towards gelatin and Daborhagin showed potent fibrinogenolytic activity. These activities were inhibited by metal chelators. Notably, the synthetic peptide inhibitors, pERW and pEKW, completely inhibit the gelatinolytic and fibrinogenolytic activities of respective SVMPs at 5 mM concentration. These complete inhibitory effects suggest that these tripeptides deserve further study for development of a therapeutic candidate for Russell’s viper envenomation. View Full-TextKeywords:
snake venom metalloproteinases; snake venom metalloproteinase inhibitors; Russell’s viper; viper venom
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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).
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MDPI and ACS Style
Yee, K.T.; Pitts, M.; Tongyoo, P.; Rojnuckarin, P.; Wilkinson, M.C. Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom. Toxins 2017, 9, 15.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.
