Ontology highlight
ABSTRACT:
PROVIDER: PRJNA902033 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR22306546_1.fastq.gz | Fastqsanger.gz | |||
| SRR22306546_2.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 2 of 2 |
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Project description:Most species of bee are capable of delivering a defensive sting which is often painful. A solitary lifestyle is the ancestral state of bees and most extant species are solitary, but information on bee venoms comes predominantly from studies on eusocial species. In this study we investigated the venom composition of the Australian great carpenter bee, Xylocopa aruana Ritsema, 1876. We show that the venom is relatively simple, composed mainly of one small amphipathic peptide (XYTX1-Xa1a), with lesser amounts of an apamin homologue (XYTX2-Xa2a) and a venom phospholipase-A2 (PLA2). XYTX1-Xa1a is homologous to, and shares a similar mode-of-action to melittin and the bombilitins, the major components of the venoms of the eusocial Apis mellifera (Western honeybee) and Bombus spp. (bumblebee), respectively. XYTX1-Xa1a and melittin directly activate mammalian sensory neurons and cause spontaneous pain behaviours in vivo, effects which are potentiated in the presence of venom PLA2. The apamin-like peptide XYTX2-Xa2a was a relatively weak blocker of small conductance calcium-activated potassium (KCa) channels and, like A. mellifera apamin and mast cell-degranulating peptide, did not contribute to pain behaviours in mice. While the composition and mode-of-action of the venom of X. aruana are similar to that of A. mellifera, the greater potency, on mammalian sensory neurons, of the major pain-causing component in A. mellifera venom may represent an adaptation to the distinct defensive pressures on eusocial Apidae.
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Project description:We describe the first comprehensive venom profile of a solitary bee, the European carpenter bee Xylocopa violacea, by using a combined proteo-transcriptomic approach. Transcripts of the venom system are used as specific database to match peptide sequences from mass spectrometry analyses of venom from dissected venom glands and venom injected during a defensive sting. In our analyses, we only discuss the proteo-transcriptomically supported venom components and reveal a diverse venom profile with 43 different protein families of which 32 are identified in the injected venom.
2023-06-26 | PXD030997 | Pride
Project description:Limacodidae is a family of lepidopteran insects comprising more than 1,500 species, over half of which produce pain-inducing defensive venom components in the larval stage, but little is known about their venom. 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 confirmed 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 their geographic separation. One notable difference is the presence of RF-amide peptide toxins in A. stimulea venom. Synthetic versions of these RF-amide toxins displayed potent activation of the human neuropeptide FF1 receptor, insecticidal activity when injected into Drosophila melanogaster, and moderate ability to inhibit the larval development of the parasitic nematode Haemonchus contortus. This study provides insights into venom evolution and toxin activity in Limacodidae, and will allow the synthetic production of A. stimulea peptide toxins towards functional and structural characterisation.
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Project description:Caterpillars of moths in the family Limacodidae produce pain-inducing defensive venoms that have evolved independently to previously characterised lepidopteran venoms, but their composition and mechanism of action are unknown. Here, we examine the limacodid venom system using the species Doratifera vulnerans as a model. Large secretory cells at the base of each spine produce a complex venom (151 proteinaceous toxins in 59 families) that consists predominantly of peptides <10 kDa. Three abundant families of venom peptides (vulnericins) are analogues of adipokinetic hormone/corazonin-like neurohormone that activate the endogenous receptor with picomolar efficacy (Family 1); cationic peptides related to cecropin that disrupt lipid bilayers, induce pain, and kill bacteria and helminths (Family 2); and disulfide-rich knottins (Family 3). Our data reveal convergent molecular evolution between limacodids, hymenopterans, and arachnids, and highlight the potential of Limacodidae for peptide biodiscovery.
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