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全面了解寄生蜂拟寄蝇毒液蛋白的一级结构。

Towards a comprehensive view of the primary structure of venom proteins from the parasitoid wasp Pimpla hypochondriaca.

作者信息

Parkinson Neil M, Conyers Christine, Keen Jeff, MacNicoll Alan, Smith Ian, Audsley Neil, Weaver Robert

机构信息

Central Science Laboratory, Sand Hutton, York YO41 1LZ, UK.

出版信息

Insect Biochem Mol Biol. 2004 Jun;34(6):565-71. doi: 10.1016/j.ibmb.2004.03.003.

Abstract

Venom from the parasitoid wasp Pimpla hypochondriaca has potent in vivo activity against insect haemocytes and disrupts host immune responses. Using hybridisation techniques, and more recently random sequence analysis, we had previously identified cDNAs encoding 10 venom proteins from this wasp and deduced their primary structures. We have now extended the random sequence analysis and discovered a further nine cDNAs encoding proteins with predicted signal sequences. The mature proteins were calculated to have masses of between 4 and 22 kDa. Post-signal sequence residues predicted from the cDNAs matched those derived by Edman degradation from venom proteins separated using gel filtration and reverse phase chromatography, confirming that the cloned cDNAs encode proteins which are secreted into the venom sac. Proteins containing at least six cysteine residues were abundant and seven of these cysteine-rich venom proteins, cvp1-7, were identified. The sequences of some of these proteins were similar, or contained similar cysteine arrangements, to Kunitz type protease inhibitors, pacifastin, the trypsin inhibitor domain protein family, atracotoxin and omega-conotoxin, respectively, which occur in a diverse range of animals including spiders, molluscs, humans and grasshoppers. Two small venom proteins, svp1 and svp2, as well as cvp7 did not have similar sequences to proteins in the GenBank protein database suggesting they may be highly specialised venom components. The random sequencing approach has provided a rapid means of determining the primary structure of the majority of Pimpla hypochondriaca venom proteins.

摘要

寄生黄蜂(Pimpla hypochondriaca)的毒液对昆虫血细胞具有强大的体内活性,并会破坏宿主的免疫反应。利用杂交技术以及最近的随机序列分析,我们之前已鉴定出编码该黄蜂10种毒液蛋白的cDNA,并推导了它们的一级结构。现在,我们扩展了随机序列分析,又发现了另外9个编码具有预测信号序列的蛋白质的cDNA。计算得出这些成熟蛋白的质量在4至22 kDa之间。从cDNA预测的信号序列后残基与通过埃德曼降解法从经凝胶过滤和反相色谱分离的毒液蛋白中获得的残基相匹配,这证实了克隆的cDNA编码分泌到毒囊中 的蛋白质。含有至少6个半胱氨酸残基的蛋白质很丰富,并且鉴定出了其中7种富含半胱氨酸的毒液蛋白,即cvp1 - 7。这些蛋白质中的一些序列分别与库尼茨型蛋白酶抑制剂、太平洋蝮蛇毒素、胰蛋白酶抑制剂结构域蛋白家族、黑寡妇蜘蛛毒素和ω - 芋螺毒素相似,或含有相似的半胱氨酸排列方式,这些毒素存在于包括蜘蛛、软体动物、人类和蚱蜢在内的多种动物中。两种小毒液蛋白svp1和svp2,以及cvp7,其序列与GenBank蛋白质数据库中的蛋白质不相似,这表明它们可能是高度特化的毒液成分。随机测序方法为确定大多数Pimpla hypochondriaca毒液蛋白的一级结构提供了一种快速手段。

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