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A Review and Database of Snake Venom Proteomes

Advances in the last decade combining transcriptomics with established proteomics methods have made possible rapid identification and quantification of protein families in snake venoms. Although over 100 studies have been published, the value of this information is increased when it is collated, all...

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Autores principales: Tasoulis, Theo, Isbister, Geoffrey K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5618223/
https://www.ncbi.nlm.nih.gov/pubmed/28927001
http://dx.doi.org/10.3390/toxins9090290
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author Tasoulis, Theo
Isbister, Geoffrey K.
author_facet Tasoulis, Theo
Isbister, Geoffrey K.
author_sort Tasoulis, Theo
collection PubMed
description Advances in the last decade combining transcriptomics with established proteomics methods have made possible rapid identification and quantification of protein families in snake venoms. Although over 100 studies have been published, the value of this information is increased when it is collated, allowing rapid assimilation and evaluation of evolutionary trends, geographical variation, and possible medical implications. This review brings together all compositional studies of snake venom proteomes published in the last decade. Compositional studies were identified for 132 snake species: 42 from 360 (12%) Elapidae (elapids), 20 from 101 (20%) Viperinae (true vipers), 65 from 239 (27%) Crotalinae (pit vipers), and five species of non-front-fanged snakes. Approximately 90% of their total venom composition consisted of eight protein families for elapids, 11 protein families for viperines and ten protein families for crotalines. There were four dominant protein families: phospholipase A(2)s (the most common across all front-fanged snakes), metalloproteases, serine proteases and three-finger toxins. There were six secondary protein families: cysteine-rich secretory proteins, l-amino acid oxidases, kunitz peptides, C-type lectins/snaclecs, disintegrins and natriuretic peptides. Elapid venoms contained mostly three-finger toxins and phospholipase A(2)s and viper venoms metalloproteases, phospholipase A(2)s and serine proteases. Although 63 protein families were identified, more than half were present in <5% of snake species studied and always in low abundance. The importance of these minor component proteins remains unknown.
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spelling pubmed-56182232017-09-29 A Review and Database of Snake Venom Proteomes Tasoulis, Theo Isbister, Geoffrey K. Toxins (Basel) Review Advances in the last decade combining transcriptomics with established proteomics methods have made possible rapid identification and quantification of protein families in snake venoms. Although over 100 studies have been published, the value of this information is increased when it is collated, allowing rapid assimilation and evaluation of evolutionary trends, geographical variation, and possible medical implications. This review brings together all compositional studies of snake venom proteomes published in the last decade. Compositional studies were identified for 132 snake species: 42 from 360 (12%) Elapidae (elapids), 20 from 101 (20%) Viperinae (true vipers), 65 from 239 (27%) Crotalinae (pit vipers), and five species of non-front-fanged snakes. Approximately 90% of their total venom composition consisted of eight protein families for elapids, 11 protein families for viperines and ten protein families for crotalines. There were four dominant protein families: phospholipase A(2)s (the most common across all front-fanged snakes), metalloproteases, serine proteases and three-finger toxins. There were six secondary protein families: cysteine-rich secretory proteins, l-amino acid oxidases, kunitz peptides, C-type lectins/snaclecs, disintegrins and natriuretic peptides. Elapid venoms contained mostly three-finger toxins and phospholipase A(2)s and viper venoms metalloproteases, phospholipase A(2)s and serine proteases. Although 63 protein families were identified, more than half were present in <5% of snake species studied and always in low abundance. The importance of these minor component proteins remains unknown. MDPI 2017-09-18 /pmc/articles/PMC5618223/ /pubmed/28927001 http://dx.doi.org/10.3390/toxins9090290 Text en © 2017 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 Review
Tasoulis, Theo
Isbister, Geoffrey K.
A Review and Database of Snake Venom Proteomes
title A Review and Database of Snake Venom Proteomes
title_full A Review and Database of Snake Venom Proteomes
title_fullStr A Review and Database of Snake Venom Proteomes
title_full_unstemmed A Review and Database of Snake Venom Proteomes
title_short A Review and Database of Snake Venom Proteomes
title_sort review and database of snake venom proteomes
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5618223/
https://www.ncbi.nlm.nih.gov/pubmed/28927001
http://dx.doi.org/10.3390/toxins9090290
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