Literature DB >> 32087377

Venomics of the asp viper Vipera aspis aspis from France.

Julien Giribaldi1, Taline Kazandjian2, Fernanda G Amorim3, Gareth Whiteley2, Simon C Wagstaff4, Guillaume Cazals1, Christine Enjalbal1, Loïc Quinton3, Nicholas R Casewell2, Sebastien Dutertre5.   

Abstract

The asp viper Vipera aspis aspis is a venomous snake found in France, and despite its medical importance, the complete toxin repertoire produced is unknown. Here, we used a venomics approach to decipher the composition of its venom. Transcriptomic analysis revealed 80 venom-annotated sequences grouped into 16 gene families. Among the most represented toxins were snake venom metalloproteases (23%), phospholipases A2 (15%), serine proteases (13%), snake venom metalloprotease inhibitors (13%) and C-type lectins (12%). LC-MS of venoms revealed similar profiles regardless of the method of extraction (milking vs defensive bite). Proteomic analysis validated 57 venom-annotated transcriptomic sequences (>70%), including one for each of the 16 families, but also identified 7 sequences not initially annotated as venom proteins, including a serine protease, a disintegrin, a glutaminyl-peptide cyclotransferase, a proactivator polypeptide-like and 3 aminopeptidases. Interestingly, phospholipases A2 were the dominant proteins in the venom, among which included an ammodytoxin B-like sequence, which may explain the reported neurotoxicity following some asp viper envenomations. In total, 87 sequences were retrieved from the Vipera aspis aspis transcriptome and proteome, constituting a valuable resource that will help in understanding the toxinological basis of clinical signs of envenoming and for the mining of useful pharmacological compounds. BIOLOGICAL SIGNIFICANCE: The asp viper (Vipera aspis aspis) causes several hundred envenomations annually in France, including unusual cases with neurological signs, resulting in one death per year on average. Here, we performed a proteotranscriptomic analysis of V. a. aspis venom in order to provide a better understanding of its venom composition. We found that, as in other Vipera species, phospholipase A2 dominates in the venom, and the presence of a sequence related to ammodytoxin B may explain the reported neurotoxicity following some asp viper envenomations. Thus, this study will help in informing the toxinological basis of clinical signs of envenoming.
Copyright © 2020 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Proteomics; Snake; Toxin; Transcriptomics; Venom; Vipera

Mesh:

Substances:

Year:  2020        PMID: 32087377     DOI: 10.1016/j.jprot.2020.103707

Source DB:  PubMed          Journal:  J Proteomics        ISSN: 1874-3919            Impact factor:   4.044


  4 in total

1.  Venomics Approach Reveals a High Proportion of Lactrodectus-Like Toxins in the Venom of the Noble False Widow Spider Steatoda nobilis.

Authors:  John P Dunbar; Antoine Fort; Damien Redureau; Ronan Sulpice; Michel M Dugon; Loïc Quinton
Journal:  Toxins (Basel)       Date:  2020-06-18       Impact factor: 4.546

2.  Venom-Induced Blood Disturbances by Palearctic Viperid Snakes, and Their Relative Neutralization by Antivenoms and Enzyme-Inhibitors.

Authors:  Abhinandan Chowdhury; Christina N Zdenek; Matthew R Lewin; Rebecca Carter; Tomaž Jagar; Erika Ostanek; Hannah Harjen; Matt Aldridge; Raul Soria; Grace Haw; Bryan G Fry
Journal:  Front Immunol       Date:  2021-06-10       Impact factor: 7.561

Review 3.  Old World Vipers-A Review about Snake Venom Proteomics of Viperinae and Their Variations.

Authors:  Maik Damm; Benjamin-Florian Hempel; Roderich D Süssmuth
Journal:  Toxins (Basel)       Date:  2021-06-17       Impact factor: 4.546

4.  A Combined Transcriptomics and Proteomics Approach Reveals the Differences in the Predatory and Defensive Venoms of the Molluscivorous Cone Snail Cylinder ammiralis (Caenogastropoda: Conidae).

Authors:  Samuel Abalde; Sébastien Dutertre; Rafael Zardoya
Journal:  Toxins (Basel)       Date:  2021-09-10       Impact factor: 4.546

  4 in total

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