Lachesis muta (Viperidae) cDNAs reveal diverging pit viper molecules and scaffolds typical of cobra (Elapidae) venoms:: Implications for snake toxin repertoire evolution
Lachesis muta (Viperidae) cDNAs reveal diverging pit viper molecules and scaffolds typical of cobra (Elapidae) venoms:: Implications for snake toxin repertoire evolution
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DOI：
10.1534/genetics.106.056515
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发表时间：
2006-06-01
期刊：
影响因子：
3.3
通讯作者：
Diniz, Marcelo R. V.
中科院分区：
文献类型：
--
作者：
Junqueira-de-Azevedo, Inacio L. M.;Ching, Ana T. C.;Diniz, Marcelo R. V.
描述毒蛇两大科（蝰蛇科和眼镜蛇科）毒素的努力通常揭示属于少数结构类型的蛋白质，特别是每个科的蛋白质。在这里，我们进行了努力，以确定罕见的cDNA，代表可能的新毒素Lachesis穆塔（蝰蛇科）。除了9类典型毒素外，迄今为止在研究的数百种蝰蛇科蛇中从未观察到的非典型分子高度表达：一种与蝰蛇科毒素有关但似乎独立起源的分歧G型凝集素;一种ohanin样毒素，这将是最近描述的眼镜蛇科毒素类的第三个成员，与人类亲酪蛋白和B30.2蛋白有关;以及一种3FTx样毒素，它是广泛研究的三指蛋白家族的新成员，包括主要的Elapidae神经毒素和CD 59抗原。这些常见和不常见的分子的存在表明，家庭之间的毒素库可能比已经被认为是更保守的，它们的功能表明毒液进化的动态过程，通过分子机制，如多个招聘的重要支架和旁系同源物之间的结构域交换，总是保持最低限度的性质，在大多数毒素结构，反对他们的非毒素对应。
Efforts to describe toxins from the two major families of venomous snakes (Viperidae and Elapidae) usually reveal proteins belonging to few structural types, particular of each family. Here we carried on an effort to determine uncommon cDNAs that represent possible new toxins from Lachesis muta (Viperidae). In addition to nine classes of typical toxins, atypical molecules never observed in the hundreds of Viperidae snakes studied so far are highly expressed: a diverging G-type lectin that is related to Viperidae toxins but appears to be independently originated; an ohanin-like toxin, which would be the third member of the most recently described class of Elapidae toxins, related to human butyrophilin and B30.2 proteins; and a 3FTx-like toxin, a new member of the widely studied three-finger family of proteins, which includes major Elapidae neurotoxins and CD59 antigen. The presence of these common and uncommon molecules suggests that the repertoire of toxins could be more conserved between families than has been considered, and their features indicate a dynamic process of venom evolution through molecular mechanisms, such as multiple recruitments of important scaffolds and domain exchange between paralogs, always keeping a minimalist nature in most toxin structures in opposition to their nontoxin counterparts.