Abstract

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 A2s (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 A2s and viper venoms metalloproteases, phospholipase A2s 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.

Highlights

  • Significant venomous snakes are almost entirely front-fanged, and are classified into three families: Atractaspidae (Burrowing Asps, 69 species), Elapidae (Elapids, 360 species), and Viperidae (Vipers, 340 species)

  • A total of 63 protein families were identified in the venoms of the 132 snake species included in this review

  • As the venom composition of only five species of non-front-fanged snake species were found, we will focus on the 127 species of front-fanged snakes, which contain 59 different protein families

Read more

Summary

Introduction

Significant venomous snakes are almost entirely front-fanged, and are classified into three families: Atractaspidae (Burrowing Asps, 69 species), Elapidae (Elapids, 360 species), and Viperidae (Vipers, 340 species). Different toxins in snake venoms, as well as the ability to rapidly measure their relative abundance These technological advances have fortuitously coincided with major improvements in our liquid chromatography (RP-HPLC),relationships and mass spectrometry (MS), identification understanding of snake evolutionary (phylogeny). Ashas theenabled venomrapid proteomes of over 100 of different toxins in snake venoms, as well as the ability to rapidly measure their relative snake species have been published, there is a sufficient number of studies to allow the general abundance. This review collects all the studies over 100 snake species have been published, there is a sufficient number of studies to allow the published in the last ten years that provide relatively complete compositional abundances of the general themes in snake venom evolution to begin to be understood. Compositional venom studies were identified for 132 species of snakes: 42 species from 360

Results
Discussion
Dominant Protein Families
Secondary Protein Families
Major Inter-Family Differences
Elapids
Vipers
Differences
Medical
Evolutionary Biology
Findings
Methods
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call