Peptidome and transcriptome analysis of the toxin-like peptides in the venom glands of Tarantula Grammostora rosea
Peptidome and transcriptome analysis of the toxin-like peptides in the venom glands of Tarantula Grammostora rosea
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狼蛛毒腺中毒素样肽的肽组和转录组分析
DOI：
10.1007/978-94-007-6646-4_13-1
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
T.
中科院分区：
文献类型：
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作者：
Kimura;T.;& Kubo;T.
狼蛛的毒腺能产生多种生物活性肽。智利普通狼蛛Grammostola rosea具有相对较大的毒腺，分泌的毒液和毒腺已分别用于蛋白质组学和基因组学方法。表达序列标签分析的cDNA文库已经揭示了48毒素样肽从狼蛛的日期。其中24个毒素为抑制性胱氨酸结基序肽（GTx 1和GTx 2），11个肽（GTx 3）为曼巴肠毒素1（MIT 1）样肽，7个为GTx 4类似于从另一种狼蛛中鉴定的ESTX样肽。还鉴定了类似于JZTX-64、适体毒素、CRISP或TCTP的肽。GTx 3系列具有在脊椎动物MIT 1，Bv 8，prokineticins和无脊椎动物astakines中保守的半胱氨酸框架，而这些肽据报道具有多种生物活性，如肌肉收缩，血管生成等。GTx-CRISP是第一个从节肢动物vemon中鉴定的CRISP样蛋白。GTx 1 -15与从另一种蜘蛛中分离的phrixotoxin 3（PaurTx 3）具有76.5%的同源性。PaurTx 3的特点是阻断钠通道;然而，GTx 1 -15优先抑制T型电压依赖性钙通道。计算机二级和三级结构预测显示，GTx 1 -15和PaurTx 3，以及其他钠通道阻断剂如海南毒素-IV和ceratotoxin 2，显示出非常相似的β-链组成，最佳对接区域的分布和表面静电势。研究结果可能表明，这些肽毒素是在进化压力下通过基因复制从共同祖先进化而来的，以维持适合靶向低压依赖性离子通道的表面环境。
Tarantula venom glands produce a large variety of bioactive peptides. Chilean common tarantula Grammostola rosea has relatively large venom glands, and the secreted venom and the venom glands have been utilized in both proteomic and genomic approaches, respectively. The expressed sequence tag analysis for the cDNA library has unveiled 48 toxin-like peptides from the tarantula to date. Among them, 24 toxins are inhibitor cystine knot motif peptides (GTx1 and GTx2), 11 peptides (GTx3) are mamba intestinal toxin 1 (MIT1)-like peptides, and 7 are GTx4s similar to ESTX-like peptides identified from another tarantula species. Peptides similar to JZTX-64, aptotoxin, CRISP, or TCTP were also identified. GTx3 series possess a cysteine framework that is conserved among vertebrate MIT1, Bv8, prokineticins, and invertebrate astakines, while these peptides are reported to have diverse bioactivities such as muscle contractions, angiogenesis, etc. GTx-CRISP is the first CRISP-like protein identified from the arthropod vemon. A novel peptide, named GTx1-15, shows 76.5% sequence homology with phrixotoxin 3 (PaurTx3) isolated from another spider. PaurTx3 was characterized to block sodium channels; however, GTx1-15 preferentially inhibited T-type voltage-dependent calcium channels. Secondary and tertiary structure prediction in silico revealed that GTx1-15 and PaurTx3, and other sodium channel blockers such as hainantoxin-IV and ceratotoxin 2 as well, show very similar β-strand composition, distribution of optimal docking areas, and surface electrostatic potential. The findings may suggest that these peptide toxins evolved from common ancestors by gene duplication under evolution pressures to maintain surface environment appropriate for targeting low-voltage-dependent ion channels.