Article (Périodiques scientifiques)
Venomics of the asp viper Vipera aspis aspis from France
Giribaldi, J.; Kazandjian, T.; Amorim, F. G. et al.
2020In Journal of Proteomics, 218
Peer reviewed vérifié par ORBi
 

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Mots-clés :
Proteomics; Snake; Toxin; Transcriptomics; Venom; Vipera
Résumé :
[en] 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. © 2020 Elsevier B.V.
Disciplines :
Chimie
Auteur, co-auteur :
Giribaldi, J.;  Institut des Biomolécules Max Mousseron, UMR 5247, Univ Montpellier, CNRS, Place Eugène Bataillon, Montpellier CEDEX 5, 34095, France
Kazandjian, T.;  Centre for Snakebite Research and Interventions, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool, L3 5QA, United Kingdom
Amorim, F. G.;  Laboratory of Mass Spectrometry, MolSys Research Unit, University of Liège, Liège, Belgium
Whiteley, G.;  Centre for Snakebite Research and Interventions, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool, L3 5QA, United Kingdom
Wagstaff, S. C.;  Bioinformatics Unit, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool, L3 5QA, United Kingdom
Cazals, G.;  Institut des Biomolécules Max Mousseron, UMR 5247, Univ Montpellier, CNRS, Place Eugène Bataillon, Montpellier CEDEX 5, 34095, France
Enjalbal, C.;  Institut des Biomolécules Max Mousseron, UMR 5247, Univ Montpellier, CNRS, Place Eugène Bataillon, Montpellier CEDEX 5, 34095, France
Quinton, Loïc  ;  Université de Liège - ULiège > Département de chimie (sciences) > Chimie biologique
Casewell, N. R.;  Centre for Snakebite Research and Interventions, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool, L3 5QA, United Kingdom
Dutertre, S.;  Institut des Biomolécules Max Mousseron, UMR 5247, Univ Montpellier, CNRS, Place Eugène Bataillon, Montpellier CEDEX 5, 34095, France
Langue du document :
Français
Titre :
Venomics of the asp viper Vipera aspis aspis from France
Date de publication/diffusion :
2020
Titre du périodique :
Journal of Proteomics
ISSN :
1874-3919
eISSN :
1876-7737
Maison d'édition :
Elsevier
Volume/Tome :
218
Peer reviewed :
Peer reviewed vérifié par ORBi
Intitulé du projet de recherche :
ANR-16-CE34-0002; FAPESP: 2015/26609-7, 200517/Z/16/Z, 2016/20641-9
Organisme subsidiant :
ANR - Agence Nationale de la Recherche
FAPESP - Fundação de Amparo à Pesquisa do Estado de São Paulo
Wellcome Trust
Disponible sur ORBi :
depuis le 24 juin 2020

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