Insight into mosquito GnRH-related neuropeptide receptor specificity revealed through analysis of naturally occurring and synthetic analogs of this neuropeptide family

Wahedi, Azizia; GÄde, Gerd; Paluzzi, Jean‐Paul

doi:10.1101/699645

Cited by 1 publication

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References 66 publications

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“…2) and show similarity to the endogenous insect ACP neuropeptide. We applied three synthetic D. vulnerans Family 1 venom peptides to the ACP receptor (ACPR) from the mosquito Aedes aegypti (49,50) and found that two of them (hereafter indicated with prefix Z) activated the receptor with picomolar potency (Fig. 4E) while having no activity on receptors of the closely related neuropeptides adipokinetic hormone and corazonin (51,52).…”

Section: Abundant Neurohormone-like Peptides Potently Activate Insectmentioning

confidence: 99%

Production, composition, and mode of action of the painful defensive venom produced by a limacodid caterpillar, Doratifera vulnerans

Walker

Robinson

Paluzzi

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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Venoms have evolved independently several times in Lepidoptera. Limacodidae is a family with worldwide distribution, many of which are venomous in the larval stage, but the composition and mode of action of their venom is unknown. Here, we use imaging technologies, transcriptomics, proteomics, and functional assays to provide a holistic picture of the venom system of a limacodid caterpillar, Doratifera vulnerans. Contrary to dogma that defensive venoms are simple in composition, D. vulnerans produces a complex venom containing 151 proteinaceous toxins spanning 59 families, most of which are peptides <10 kDa. Three of the most abundant families of venom peptides (vulnericins) are 1) analogs of the adipokinetic hormone/corazonin-related neuropeptide, some of which are picomolar agonists of the endogenous insect receptor; 2) linear cationic peptides derived from cecropin, an insect innate immune peptide that kills bacteria and parasites by disrupting cell membranes; and 3) disulfide-rich knottins similar to those that dominate spider venoms. Using venom fractionation and a suite of synthetic venom peptides, we demonstrate that the cecropin-like peptides are responsible for the dominant pain effect observed in mammalian in vitro and in vivo nociception assays and therefore are likely to cause pain after natural envenomations by D. vulnerans. Our data reveal convergent molecular evolution between limacodids, hymenopterans, and arachnids and demonstrate that lepidopteran venoms are an untapped source of novel bioactive peptides.

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Section: Abundant Neurohormone-like Peptides Potently Activate Insectmentioning

confidence: 99%

Production, composition, and mode of action of the painful defensive venom produced by a limacodid caterpillar, Doratifera vulnerans

Walker

Robinson

Paluzzi

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

show abstract

Insight into mosquito GnRH-related neuropeptide receptor specificity revealed through analysis of naturally occurring and synthetic analogs of this neuropeptide family

Abstract: 1 specificity revealed through analysis of naturally occurring and 2 synthetic analogs of this neuropeptide family 3

Cited by 1 publication

References 66 publications

Production, composition, and mode of action of the painful defensive venom produced by a limacodid caterpillar, Doratifera vulnerans

Production, composition, and mode of action of the painful defensive venom produced by a limacodid caterpillar, Doratifera vulnerans

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