Venomics of the asp viper Vipera aspis aspis from France

Autor(es)

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]

Afiliação do(s) autor(es)

^[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

• Tipo de documento: Artigo Científico
• Fonte: JOURNAL OF PROTEOMICS; v. 218, APR 30 2020.
• Citações Web of Science: 4

Resumo

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)

• Processo FAPESP: 16/20641-9 - Integração da abordagens ômicas para obter o perfil da peçonha da serpente Bothrops moojeni: revelando novas toxinas e divergências ontogênicas
• Beneficiário: Fernanda Gobbi Amorim
• Modalidade de apoio: Bolsas no Exterior - Estágio de Pesquisa - Pós-Doutorado
• Processo FAPESP: 15/26609-7 - Venômica da serpente Bothrops moojeni: aplicação de toxinas de interesse biotecnológico obtidas por técnicas ômicas
• Beneficiário: Fernanda Gobbi Amorim
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado