Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland 4072, Australia; Australian Research Council Centre of Excellence for Innovations in Protein and Peptide Science, Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland 4072, Australia.
Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland 4072, Australia; Australian Research Council Centre of Excellence for Innovations in Protein and Peptide Science, Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland 4072, Australia; Centre for Inflammation and Disease Research, The University of Queensland, St Lucia, Queensland 4072, Australia.
Biochem Pharmacol. 2023 Jul;213:115598. doi: 10.1016/j.bcp.2023.115598. Epub 2023 May 16.
Limacodidae is a family of lepidopteran insects comprising >1500 species. More than half of these species produce pain-inducing defensive venoms in the larval stage, but little is known about their venom toxins. Recently, we characterised proteinaceous toxins from the Australian limacodid caterpillar Doratifera vulnerans, but it is unknown if the venom of this species is typical of other Limacodidae. Here, we use single animal transcriptomics and venom proteomics to investigate the venom of an iconic limacodid, the North American saddleback caterpillar Acharia stimulea. We identified 65 venom polypeptides, grouped into 31 different families. Neurohormones, knottins, and homologues of the immune signaller Diedel make up the majority of A.stimulea venom, indicating strong similarities to D. vulnerans venom, despite the large geographic separation of these caterpillars. One notable difference is the presence of RF-amide peptide toxins in A. stimulea venom. Synthetic versions of one of these RF-amide toxins potently activated the human neuropeptide FF1 receptor, displayed insecticidal activity when injected into Drosophila melanogaster, and moderately inhibited larval development of the parasitic nematode Haemonchus contortus. This study provides insights into the evolution and activity of venom toxins in Limacodidae, and provides a platform for future structure-function characterisation of A.stimulea peptide toxins.
长鼻目科是鳞翅目昆虫的一个科，包含超过 1500 种。这些物种中有一半以上在幼虫阶段产生引起疼痛的防御性毒液，但对它们的毒液毒素知之甚少。最近，我们从澳大利亚 Limacodidae 毛毛虫 Doratifera vulnerans 中鉴定出了蛋白质毒素，但尚不清楚该物种的毒液是否具有代表性。在这里，我们使用单个动物转录组学和毒液蛋白质组学来研究北美鞍背毛毛虫 Acharia stimulea 的毒液。我们鉴定出 65 种毒液多肽，分为 31 个不同的家族。神经激素、knottins 和免疫信号分子 Diedel 的同源物构成了 A.stimulea 毒液的主要成分，表明与 D. vulnerans 毒液具有很强的相似性，尽管这些毛毛虫在地理上相距甚远。一个值得注意的区别是 A. stimulea 毒液中存在 RF-酰胺肽毒素。这些 RF-酰胺毒素之一的合成版本能够强烈激活人类神经肽 FF1 受体，在注射入果蝇时表现出杀虫活性，并适度抑制寄生线虫 Haemonchus contortus 的幼虫发育。这项研究提供了关于 Limacodidae 毒液毒素进化和活性的见解，并为未来 A.stimulea 肽毒素的结构功能特征提供了一个平台。
