Institut des Biomolécules Max Mousseron, UMR 5247, Univ Montpellier, CNRS, Place Eugène Bataillon, 34095 Montpellier CEDEX 5, France.
Centre for Snakebite Research and Interventions, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool L3 5QA, UK.
J Proteomics. 2020 Apr 30;218:103707. doi: 10.1016/j.jprot.2020.103707. Epub 2020 Feb 19.
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.
圆斑蝰(Vipera aspis aspis)是一种在法国发现的毒蛇,尽管其具有医学重要性,但完全未知其产生的毒素组成。在这里,我们使用毒理学方法来解析其毒液的组成。转录组分析显示,有 80 种与毒液相关的序列被分为 16 个基因家族。其中最具代表性的毒素包括蛇毒金属蛋白酶(23%)、磷脂酶 A2(15%)、丝氨酸蛋白酶(13%)、蛇毒金属蛋白酶抑制剂(13%)和 C 型凝集素(12%)。无论采用哪种提取方法(挤奶或防御性咬伤),LC-MS 分析均揭示了相似的图谱。蛋白质组学分析验证了 57 种与毒液相关的转录组序列(>70%),其中包括 16 个家族中的每一个,但也鉴定出 7 种最初未被注释为毒液蛋白的序列,包括一种丝氨酸蛋白酶、一种分裂素、一种谷氨酰肽环转移酶、一种前激活物多肽样物和 3 种氨肽酶。有趣的是,磷脂酶 A2 是毒液中的主要蛋白,其中包括一种类似 ammodytoxin B 的序列,这可能解释了一些圆斑蝰蛇咬伤后的神经毒性。总共从圆斑蝰(Vipera aspis aspis)转录组和蛋白质组中检索到 87 种序列,构成了有价值的资源,将有助于了解中毒症状的毒理学基础,并用于挖掘有用的药理学化合物。生物学意义:圆斑蝰(Vipera aspis aspis)每年在法国造成数百人中毒,包括一些不常见的神经症状病例,平均每年有 1 人死亡。在这里,我们对 V. a. aspis 毒液进行了蛋白质组学分析,以更好地了解其毒液组成。我们发现,与其他蝰蛇属物种一样,磷脂酶 A2 在毒液中占主导地位,存在与 ammodytoxin B 相关的序列可能解释了一些圆斑蝰蛇咬伤后的神经毒性。因此,这项研究将有助于阐明中毒症状的毒理学基础。