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Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom
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 moda...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5308247/ https://www.ncbi.nlm.nih.gov/pubmed/28042812 http://dx.doi.org/10.3390/toxins9010015 |
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author | Yee, Khin Than Pitts, Morgan Tongyoo, Pumipat Rojnuckarin, Ponlapat Wilkinson, Mark C. |
author_facet | Yee, Khin Than Pitts, Morgan Tongyoo, Pumipat Rojnuckarin, Ponlapat Wilkinson, Mark C. |
author_sort | Yee, Khin Than |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5308247 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-53082472017-02-14 Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom Yee, Khin Than Pitts, Morgan Tongyoo, Pumipat Rojnuckarin, Ponlapat Wilkinson, Mark C. Toxins (Basel) Article 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. MDPI 2016-12-30 /pmc/articles/PMC5308247/ /pubmed/28042812 http://dx.doi.org/10.3390/toxins9010015 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Yee, Khin Than Pitts, Morgan Tongyoo, Pumipat Rojnuckarin, Ponlapat Wilkinson, Mark C. Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom |
title | Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom |
title_full | Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom |
title_fullStr | Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom |
title_full_unstemmed | Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom |
title_short | Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom |
title_sort | snake venom metalloproteinases and their peptide inhibitors from myanmar russell’s viper venom |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5308247/ https://www.ncbi.nlm.nih.gov/pubmed/28042812 http://dx.doi.org/10.3390/toxins9010015 |
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