Studies on the venom proteome of Bothrops asper: Perspectives and applications
Studies on the venom proteome of Bothrops asper: Perspectives and applications
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DOI：
10.1016/j.toxicon.2009.06.011
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发表时间：
2009-12-01
期刊：
影响因子：
2.8
通讯作者：
Calvete, Juan J.
中科院分区：
文献类型：
--
作者：
Alape-Giron, Alberto;Flores-Diaz, Marietta;Calvete, Juan J.
Bothrops asper是中美洲绝大多数蛇咬伤事故的罪魁祸首，几项研究表明，其毒液的特定毒性和酶活性随标本的地理来源和年龄而变化。自1964年以来，已报道了来自加勒比海和太平洋哥斯达黎加的标本之间的毒液蛋白质和酶的变异。最近，我们进行了比较蛋白质组学特征的毒液从一个人口的每一个versant。属于几个家族的蛋白质，包括去整合素、磷脂酶A（2）、丝氨酸蛋白酶、C型凝集素、CRISP、L-氨基酸氧化酶和Zn 2+依赖性金属蛋白酶，在两个种群的毒液中显示出不同程度的相对出现。从成人和新生儿的毒液之间的蛋白质谱的显着差异的发生，并从同一地区或发育阶段的个别标本之间的毒液样品，进一步证明了存在的地理，个体发育和个体变异的毒液蛋白质组的这个物种。这些发现为理解B的生物学提供了新的见解。Asper，有助于更深入地了解其毒液诱导的病理学，并强调了使用来自两个地区的标本的毒液混合用于生产表现出最广泛的交叉反应性的抗蛇毒血清的重要性。此外，对B的蛋白质组成的了解。蛇蛇毒为将来详细研究单个毒素的结构-功能以及开发研究治疗性抗蛇毒血清的反应性的新方案铺平了道路。(C)2009爱思唯尔有限公司版权所有。
Bothrops asper is responsible for the vast majority of snakebite accidents in Central America and several studies have demonstrated that specific toxic and enzymatic activities of its venom vary with the geographic origin and age of the specimens. Variability in venom proteins and enzymes between specimens from the Caribbean and the Pacific versants of Costa Rica has been reported since 1964. Recently, we performed a comparative proteomic characterization of the venoms from one population of each versant. Proteins belonging to several families, including disintegrin, phospholipases A(2), serine proteinases, C-type lectins, CRISP, L-amino acid oxiclase, and Zn2+-dependent metalloproteinases show a variable degree of relative occurrence in the venoms of both populations. The occurrence of prominent differences in the protein profile between venoms from adults and newborns, and among venom samples from individual specimens of the same region or developmental stage, further demonstrated the existence of geographic, ontogenetic and individual variability in the venom proteome of this species. These findings provide new insights towards understanding the biology of B. asper, contribute to a deeper understanding of the pathology induced by its venom and underscore the importance of the use of venoms pooled from specimens from both regions for producing antivenom exhibiting the broadest cross-reactivity. Furthermore, knowledge of the protein composition of B. asper venom paves the way for detailed future structure-function studies of individual toxins as well as for the development of new protocols to study the reactivity of therapeutic antivenoms. (C) 2009 Elsevier Ltd. All rights reserved.