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毒液的触须:动物界中的有毒蛋白质趋同现象

Tentacles of venom: toxic protein convergence in the Kingdom Animalia.

作者信息

Fry B G, Roelants K, Norman J A

机构信息

Department of Biochemistry and Molecular Biology, Venomics Research Laboratory, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.

出版信息

J Mol Evol. 2009 Apr;68(4):311-21. doi: 10.1007/s00239-009-9223-8. Epub 2009 Mar 18.

DOI:10.1007/s00239-009-9223-8
PMID:19294452
Abstract

The origin and evolution of venom in many animal orders remain controversial or almost entirely uninvestigated. Here we use cDNA studies of cephalopod posterior and anterior glands to reveal a single early origin of the associated secreted proteins. Protein types recovered were CAP (CRISP, Antigen 5 [Ag5] and Pathogenesis-related [PR-1]), chitinase, peptidase S1, PLA(2) (phospholipase A(2)), and six novel peptide types. CAP, chitinase, and PLA(2) were each recovered from a single species (Hapalochlaena maculosa, Octopus kaurna, and Sepia latimanus, respectively), while peptidase S1 transcripts were found in large numbers in all three posterior gland libraries. In addition, peptidase S1 transcripts were recovered from the anterior gland of H. maculata. We compare their molecular evolution to that of related proteins found in invertebrate and vertebrate venoms, revealing striking similarities in the types of proteins selected for toxic mutation and thus shedding light on what makes a protein amenable for use as a toxin.

摘要

许多动物类群中毒液的起源和演化仍存在争议,或者几乎完全未被研究。在此,我们利用对头足类动物前后腺体的cDNA研究,揭示相关分泌蛋白的单一早期起源。回收的蛋白类型包括CAP(CRISP、抗原5 [Ag5]和病程相关蛋白[PR-1])、几丁质酶、肽酶S1、PLA(2)(磷脂酶A(2))以及六种新型肽类。CAP、几丁质酶和PLA(2)分别从单一物种中回收(分别为黄斑海兔、卡氏章鱼和宽纹乌贼),而肽酶S1转录本在所有三个后腺文库中大量存在。此外,从黄斑海蛞蝓的前腺中回收了肽酶S1转录本。我们将它们的分子演化与在无脊椎动物和脊椎动物毒液中发现的相关蛋白进行比较,揭示了在选择用于毒性突变的蛋白类型方面的显著相似性,从而阐明了何种蛋白适合用作毒素。

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