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      Venomic Analysis of the Poorly Studied Desert Coral Snake, Micrurus tschudii tschudii, Supports the 3FTx/PLA 2 Dichotomy across Micrurus Venoms

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          Abstract

          The venom proteome of the poorly studied desert coral snake Micrurus tschudii tschudii was unveiled using a venomic approach, which identified ≥38 proteins belonging to only four snake venom protein families. The three-finger toxins (3FTxs) constitute, both in number of isoforms (~30) and total abundance (93.6% of the venom proteome), the major protein family of the desert coral snake venom. Phospholipases A 2 (PLA 2s; seven isoforms, 4.1% of the venom proteome), 1–3 Kunitz-type proteins (1.6%), and 1–2 l-amino acid oxidases (LAO, 0.7%) complete the toxin arsenal of M. t. tschudii. Our results add to the growing evidence that the occurrence of two divergent venom phenotypes, i.e., 3FTx- and PLA 2-predominant venom proteomes, may constitute a general trend across the cladogenesis of Micrurus. The occurrence of a similar pattern of venom phenotypic variability among true sea snake (Hydrophiinae) venoms suggests that the 3FTx/PLA 2 dichotomy may be widely distributed among Elapidae venoms.

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          A phylogeny and revised classification of Squamata, including 4161 species of lizards and snakes

          R Pyron, Frank T. Burbrink, John Wiens (2013)
          Background The extant squamates (>9400 known species of lizards and snakes) are one of the most diverse and conspicuous radiations of terrestrial vertebrates, but no studies have attempted to reconstruct a phylogeny for the group with large-scale taxon sampling. Such an estimate is invaluable for comparative evolutionary studies, and to address their classification. Here, we present the first large-scale phylogenetic estimate for Squamata. Results The estimated phylogeny contains 4161 species, representing all currently recognized families and subfamilies. The analysis is based on up to 12896 base pairs of sequence data per species (average = 2497 bp) from 12 genes, including seven nuclear loci (BDNF, c-mos, NT3, PDC, R35, RAG-1, and RAG-2), and five mitochondrial genes (12S, 16S, cytochrome b, ND2, and ND4). The tree provides important confirmation for recent estimates of higher-level squamate phylogeny based on molecular data (but with more limited taxon sampling), estimates that are very different from previous morphology-based hypotheses. The tree also includes many relationships that differ from previous molecular estimates and many that differ from traditional taxonomy. Conclusions We present a new large-scale phylogeny of squamate reptiles that should be a valuable resource for future comparative studies. We also present a revised classification of squamates at the family and subfamily level to bring the taxonomy more in line with the new phylogenetic hypothesis. This classification includes new, resurrected, and modified subfamilies within gymnophthalmid and scincid lizards, and boid, colubrid, and lamprophiid snakes.
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            Coevolution of diet and prey-specific venom activity supports the role of selection in snake venom evolution.

            Axel Barlow, Catharine Pook, Robert Harrison … (2009)
            The processes that drive the evolution of snake venom variability, particularly the role of diet, have been a topic of intense recent research interest. Here, we test whether extensive variation in venom composition in the medically important viper genus Echis is associated with shifts in diet. Examination of stomach and hindgut contents revealed extreme variation between the major clades of Echis in the proportion of arthropod prey consumed. The toxicity (median lethal dose, LD(50)) of representative Echis venoms to a natural scorpion prey species was found to be strongly associated with the degree of arthropod feeding. Mapping the results onto a novel Echis phylogeny generated from nuclear and mitochondrial sequence data revealed two independent instances of coevolution of venom toxicity and diet. Unlike venom LD(50), the speed with which venoms incapacitated and killed scorpions was not associated with the degree of arthropod feeding. The prey-specific venom toxicity of arthropod-feeding Echis may thus be adaptive primarily by reducing venom expenditure. Overall, our results provide strong evidence that variation in snake venom composition results from adaptive evolution driven by natural selection for different diets, and underscores the need for a multi-faceted, integrative approach to the study of the causes of venom evolution.
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              Structure, function and evolution of three-finger toxins: mini proteins with multiple targets.

              Robin Doley, R. Kini (2010)
              Snake venoms are complex mixtures of pharmacologically active peptides and proteins. These protein toxins belong to a small number of superfamilies of proteins. Three-finger toxins belong to a superfamily of non-enzymatic proteins found in all families of snakes. They have a common structure of three beta-stranded loops extending from a central core containing all four conserved disulphide bonds. Despite the common scaffold, they bind to different receptors/acceptors and exhibit a wide variety of biological effects. Thus, the structure-function relationships of this group of toxins are complicated and challenging. Studies have shown that the functional sites in these 'sibling' toxins are located on various segments of the molecular surface. Targeting to a wide variety of receptors and ion channels and hence distinct functions in this group of mini proteins is achieved through a combination of accelerated rate of exchange of segments as well as point mutations in exons. In this review, we describe the structural and functional diversity, structure-function relationships and evolution of this group of snake venom toxins. (c) 2010 Elsevier Ltd. All rights reserved.
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                Author and article information

                Contributors
                Stephen P. Mackessy: Role: Academic Editor
                Journal
                Journal ID (nlm-ta): Toxins (Basel)
                Journal ID (iso-abbrev): Toxins (Basel)
                Journal ID (publisher-id): toxins
                Title: Toxins
                Publisher: MDPI
                ISSN (Electronic): 2072-6651
                Publication date (Electronic): 07 June 2016
                Publication date Collection: June 2016
                Volume: 8
                Issue: 6
                Electronic Location Identifier: 178
                Affiliations
                [1 ]Laboratorio de Venómica Estructural y Funcional, Instituto de Biomedicina de Valencia, CSIC, Jaime Roig 11, Valencia 46010, Spain; libia.sanz@ 123456ibv.csic.es (L.S.); dpla@ 123456ibv.csic.es (D.P.); aperez@ 123456ibv.csic.es (A.P.); yrodriguez@ 123456ibv.csic.es (Y.R.)
                [2 ]Departamento Academico de Ciencias Celulares y Moleculares, Facultad de Ciencias y Filosofía, Universidad Peruana Cayetano Heredia, Lima 31, Perú; alfonso.zavaleta@ 123456upch.pe (A.Z.); maria.salas@ 123456upch.pe (M.S.)
                [3 ]Instituto Nacional de Salud, Ministerio de Salud, Lima 11, Perú
                [4 ]Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San Jose 11501, Costa Rica; bruno.lomonte@ 123456ucr.ac.cr
                Author notes
                [* ]Correspondence: jcalvete@ 123456ibv.csic.es ; Tel.: +34-96-339-1778; Fax: +34-96-369-0800
                Article
                Publisher ID: toxins-08-00178
                DOI: 10.3390/toxins8060178
                PMC ID: 4926144
                PubMed ID: 27338473
                SO-VID: 00590067-94c0-4bb8-a91f-5333fef11985
                Copyright © © 2016 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                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/).

                History
                Date received : 23 March 2016
                Date accepted : 01 June 2016
                Categories
                Subject: Article

                ScienceOpen disciplines: Molecular medicine
                Keywords: micrurus tschudii tschudii venom,venomics,snake venom proteome,three-finger toxin,snake venom phospholipase a2,mass spectrometry
                Data availability:
                ScienceOpen disciplines: Molecular medicine
                Keywords: micrurus tschudii tschudii venom, venomics, snake venom proteome, three-finger toxin, snake venom phospholipase a2, mass spectrometry

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