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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Venomics of the asp viper Vipera aspis aspis from France

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Author(s):
Giribaldi, Julien [1] ; Kazandjian, Taline [2] ; Amorim, Fernanda G. [3] ; Whiteley, Gareth [2] ; Wagstaff, Simon C. [4] ; Cazals, Guillaume [1] ; Enjalbal, Christine [1] ; Quinton, Loic [3] ; Casewell, Nicholas R. [2] ; Dutertre, Sebastien [1]
Total Authors: 10
Affiliation:
[1] Univ Montpellier, Inst Biomol Max Mousseron, CNRS, UMR 5247, Pl Eugene Bataillon, F-34095 Montpellier 5 - France
[2] Univ Liverpool Liverpool Sch Trop Med, Ctr Snakebite Res & Intervent, Pembroke Pl, Liverpool L3 5QA, Merseyside - England
[3] Univ Liege, MolSys Res Unit, Lab Mass Spectrometry, Liege - Belgium
[4] Univ Liverpool Liverpool Sch Trop Med, Bioinformat Unit, Pembroke Pl, Liverpool L3 5QA, Merseyside - England
Total Affiliations: 4
Document type: Journal article
Source: JOURNAL OF PROTEOMICS; v. 218, APR 30 2020.
Web of Science Citations: 4
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. (AU)

FAPESP's process: 16/20641-9 - Integration of Omics Approaches to Profile the Venom of the Bothrops moojeni snake: unreavelling new toxins and ontogenic divergences
Grantee:Fernanda Gobbi Amorim
Support Opportunities: Scholarships abroad - Research Internship - Post-doctor
FAPESP's process: 15/26609-7 - Bothrops moojeni snake venomics: application of toxins of biotechnological interest obtained by omics techniques
Grantee:Fernanda Gobbi Amorim
Support Opportunities: Scholarships in Brazil - Post-Doctoral