期刊
BIOCHEMICAL PHARMACOLOGY
卷 213, 期 -, 页码 -出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bcp.2023.115598
关键词
Venom peptide; G protein-coupled receptor; Inhibitor cystine knot; Adipokinetic hormone; corazonin-related pep; tide; Insect venom; RF-amide
This study investigates the venom composition of the North American saddleback caterpillar Acharia stimulea, and finds that it shares strong similarities with the venom of the Australian limacodid caterpillar Doratifera vulnerans. The venom of A. stimulea contains neurohormones, knottins, and homologues of the immune signaller Diedel, as well as RF-amide peptide toxins, which display various activities such as activation of human neuropeptide FF1 receptor, insecticidal activity, and inhibition of larval development in a parasitic nematode.
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.
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