Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom

Bibliographic Details
Title: Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom
Authors: Khin Than Yee, Morgan Pitts, Pumipat Tongyoo, Ponlapat Rojnuckarin, Mark C. Wilkinson
Source: Toxins, Vol 9, Iss 1, p 15 (2016)
Publisher Information: MDPI AG, 2016.
Publication Year: 2016
Collection: LCC:Medicine
Subject Terms: snake venom metalloproteinases, snake venom metalloproteinase inhibitors, Russell’s viper, viper venom, Medicine
More Details: 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.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2072-6651
Relation: http://www.mdpi.com/2072-6651/9/1/15; https://doaj.org/toc/2072-6651
DOI: 10.3390/toxins9010015
Access URL: https://doaj.org/article/5260590f572b4f46b6a48d78ae1f9a69
Accession Number: edsdoj.5260590f572b4f46b6a48d78ae1f9a69
Database: Directory of Open Access Journals
More Details
ISSN:20726651
DOI:10.3390/toxins9010015
Published in:Toxins
Language:English