Assembling an arsenal:: Origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences

Assembling an arsenal:: Origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences
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DOI:
10.1093/molbev/msh091
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发表时间:
2004-05-01
影响因子:
10.7
通讯作者:
Wüster, W
Wüster, W
中科院分区:
生物学1区
文献类型:
--
作者:
Fry, BG;Wüster, W

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我们分析了蛇毒毒素家族的起源和进化的蝰蛇和眼镜蛇的毒素和相关的非毒液蛋白的氨基酸序列的系统发育分析。在分析的8个毒素家族中,5个提供了在高级蛇多样化之前招募到蛇毒蛋白质组中的明确证据(Kunitz型蛋白酶抑制剂,CRISP毒素,半乳糖结合凝集素,M12 B肽酶,神经生长因子毒素),一个是模棱两可的(半胱氨酸蛋白酶抑制剂毒素)。在另外两种(磷脂酶A(2)和利尿钠毒素)中,毒液毒素的非单系性表明这些蛋白质在眼镜蛇和蝰蛇中的存在是由独立的募集事件引起的。ANP/BNP利尿钠毒素可能是基础的,而CNP/BPP毒素仅是蝰蛇科的。同样,凝集素也被招募了两次。与半乳糖结合凝集素的基础招募相反,C型凝集素仅显示为蝰蛇科,α链和β链来自早期复制事件。这些结果提供了强有力的额外证据,即毒液在高级蛇辐射的基础上进化一次,而不是在不同的谱系中多次进化,这些毒素也存在于“游蛇”科的毒液中。此外,它们提供了对最早的蛇毒液组成的第一次洞察,并指出了一个研究计划的方向,该计划可以阐明蛇毒蛋白质组进化的功能背景。
We analyzed the origin and evolution of snake venom toxin families represented in both viperid and elapid snakes by means of phylogenetic analysis of the amino acid sequences of the toxins and related nonvenom proteins. Out of eight toxin families analyzed, five provided clear evidence of recruitment into the snake venom proteome before the diversification of the advanced snakes (Kunitz-type protease inhibitors, CRISP toxins, galactose-binding lectins, M12B peptidases, nerve growth factor toxins), and one was equivocal (cystatin toxins). In two others (phospholipase A(2), and natriuretic toxins), the nonmonophyly of venom toxins demonstrates that presence of these proteins in elapids and viperids results from independent recruitment events. The ANP/BNP natriuretic toxins are likely to be basal, whereas the CNP/BPP toxins are Viperidae only. Similarly, the lectins were recruited twice. In contrast to the basal recruitment of the galactose-binding lectins, the C-type lectins were shown to be Viperidae only, with the alpha-chains and beta-chains resulting from an early duplication event. These results provide strong additional evidence that venom evolved once, at the base of the advanced snake radiation, rather than multiple times in different lineages, with these toxins also present in the venoms of the "colubrid" snake families. Moreover, they provide a first insight into the composition of the earliest ophidian venoms and point the way toward a research program that could elucidate the functional context of the evolution of the snake venom proteome.