The venom and telopodal defence systems of the centipede Lithobius forficatus are functionally convergent serial homologues
Ontology highlight
ABSTRACT:
INSTRUMENT(S): TripleTOF 5600
ORGANISM(S): Lithobius Forficatus
TISSUE(S): Exocrine Glandular Secretion, Leg
SUBMITTER: 
Vanessa Schendel
LAB HEAD: Eivind A.
PROVIDER: PXD025512 | Pride | 2024-05-08
REPOSITORIES: Pride
Similar Datasets
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.
2023-06-01 | PXD039980 | Pride
Project description:The Araneae order is considered one of the most successful group among venomous animals in the world. An important factor for this success is the production of venoms, a refined biological fluid rich in proteins, short peptides and cysteine-rich peptides (CRPs). These toxins may present pharmacologically relevant biological actions, as antimicrobial, antiviral and anticancer activities, for instance. Therefore, there is an increasing interest in the exploration of venom toxins for therapeutic reasons, such as drug development. However, the process of peptide sequencing and mainly the evaluation of potential biological activities of these peptides is laborious, considering the low yield of venom extraction and the high variability of toxins present in spider venoms. Here we show a robust methodology for identification, sequencing, and initial screening of potential bioactive peptides found in the venom of Acanthoscurria rondoniae. This methodology consists in a multi-omics approach involving proteomics, peptidomics and transcriptomics analyses allied to in silico predictions of antibacterial, antifungal, antiviral and anticancer activities. Through the application of this strategy, a total of 92,889 venom gland transcripts were assembled and 84 novel toxins were identified at the protein level, including 7 short peptides and 10 fully sequenced CRPs (belonging to 7 toxin families). In silico analysis revealed that 7 CRPs families have potential antimicrobial or antiviral activities, while 2 CRPs and four short peptides are potentially anticancer. Taken together, our results demonstrate an effective multi-omics strategy for the discovery of new toxins and in silico screening of potential bioactivities. This strategy may be useful in toxin discovery, as well as in the screening of activities for the vast diversity of molecules produced by venomous animals.
2020-07-20 | PXD019343 | Pride
Project description:Prey-specialised spiders are adapted to capture specific prey items, including dangerous prey such as ants, termites or other spiders. It has been observed that the venoms of specialists are often prey-specific and less complex than those of generalists, but venom composition has not been studied in detail in prey-specialised spiders. Here, we investigated the venom of the prey-specialised white-tailed spider (Lamponidae: Lampona sp.), which utilises specialised morphological and behavioural adaptations to capture spider prey. We hypothesised Lampona spiders also possess venomic adaptations, specifically, its venom is more effective to focal spider prey due to the presence of prey-specific toxins. We analysed the venom composition using proteo-transcriptomics and taxon-specific toxicity using venom bioassays. Our analysis identified 208 putative toxin sequences, comprising 103 peptides <10 kDa and 105 proteins >10 kDa. Most peptides belonged to one of two families characterised by scaffolds containing eight or ten cysteine residues. Protein toxins showed similarity to galectins, leucine-rich repeat proteins, trypsins and neprilysins. The venom of Lampona was shown to be spider-specific, as it was more potent against the preferred spider prey than against alternative prey represented by a cricket. In contrast, the venom of a related generalist (Gnaphosidae: Gnaphosa sp.) was similarly potent against both prey types. Prey-specific Lampona toxins were found to form part of the protein (>10 kDa) fraction of the venom. These data provide insights into the molecular adaptations of venoms produced by prey-specialised spiders.
2023-02-08 | PXD033502 | Pride
Project description:Spider venoms are a unique source of bioactive peptides displaying remarkable structural stability and potent neuroactivity. Phoneutria nigriventer, often referred to as Brazilian wandering spider, banana spider or “armed” spider, is endemic from South America and amongst the most dangerous venomous spiders in the world. Envenomation accidents with P. nigriventer often occur in Brazil with approximately 4,000 cases per year and which symptoms include priapism, hypertension, blurred vision, sweating, and vomiting, amongst others. Besides its clinical relevance, P. nigriventer venom comprises promising peptide drug leads providing therapeutic effects in a range of disease models. In this study, we further explored the neuroactivity and molecular diversity of the venom from P. nigriventer using fractionation-guided high-throughput cellular assays coupled to proteomics analysis and multi-pharmacology activity to broaden the knowledge and therapeutic potential of this venom, as well as a proof-of-concept for an investigative pipeline to study spider-venom derived neuroactive peptides. We applied ion channel assays in a neuroblastoma cell line to investigate modulation of voltage-gated sodium and calcium channels, and nicotinic acetylcholine α7 receptor. We then investigated the venom components using mass spectrometry to identify peptide masses and sequences associated to the observed neuromodulations. Our findings showed this venom is highly complex compared to other neurotoxin-rich venoms and comprises potent modulators of voltage-gated sodium and calcium channels which were classified into 4 families of neuroactive peptides based on their activities and structures. In addition to the reported P. nigriventer neuroactive peptides, we identified at least 27 novel cysteine-rich venom peptides in which neuroactivities are still to be elucidated in voltage-gated ion channels and other potential targets. Our findings provide a new basis for studying non-explored bioactivities of known and novel neuroactive components in P. nigriventer venom, and further supports the successful application of our discovery pipeline for identifying ion channel-targeting venom peptides with potential to become drug leads with diverse exploratory and therapeutic applications.
2023-02-09 | PXD037904 | Pride
Project description:Insects mount an innate immune response to defend against the foreign invading microorganisms and parasites. To be successful parasites, endoparasitoid wasps need to be able to suppress the immune responses of their hosts. This allows the wasp eggs to hatch and the larvae to develop inside the host. However, the molecular mechanism underlying the interaction between wasp and its host remains largely unknown. In this study, we identified the reprolysin type metalloprotease venom component MmV189, which was designated venom regulatory factor-1 (VRF1). VRF1 plays a critical role in the interaction between the wasp Microplitis mediator and its lepidopteran host Helicoverpa armigera (the cotton bollworm). Proteomics analysis based on isobaric tags for relative and absolute quantitation (iTRAQ) revealed that at least twelve wasp venom proteins were released into the host hemolymph, causing significant changes in 511 host proteins at 24 h post parasitization. Taking an approach of integrated transcriptome and proteome analysis, we identified 313 putative proteins from the wasp venom reservoirs, 25 of which belong to the family of metalloproteases. Proenzyme of VRF1 was firstly cleaved in the host hemolymph after parasitization and then entered the hemocytes. Additionally, depletion of VRF1 in M. mediator by dsRNA-mediated knockdown significantly reduced the percentage of cocoon formation. Furthermore, we showed possible binding of VRF1 to Dorsal, a H. armigera nuclear factor kappa B (NF-κB), using yeast two-hybrid and pull-down assays, and confirmed the cleavage of Dorsal by VRF1. Moreover, we found that VRF1 acts as a protease to process Dorsal in the host hemocytes and suppress the induction of antimicrobial peptides (AMPs). Taken together, our findings identify a novel mechanism by which a component of endoparasitoid wasp venom interferes with host immune signaling cascades.
2019-01-07 | PXD007905 | Pride
Project description:While cellular transcripts encode rich information that provide key features to understand the molecular basis of snake venom variation, their presence/ abundance does not necessary imply/correlate in the translation of a functional (protein) product. In this study we carried out an analysis of the venom gland proteome of Bothrops jararaca taking into account two distinct phases of its ontogenetic development (i.e. newborn and adult specimens) and the marked sexual dimorphism recently reported on its venom proteome. Proteomic data analysis showed wider dynamic range for toxins when comparing to non-toxins and a dynamic proteome rearrangement in cellular proteins upon B. jararaca development. Differentially expressed proteins covered a number of biological pathways related to protein synthesis, including proteins related to transcription and translation, which were found to be significantly higher expressed in the newborn venom gland. Our results showed that the variation in the expression levels of cellular proteins gives rise to an even higher variation in the dynamic range of the expressed toxins. Upon ageing, the molecular constraints related to protein synthesis together with ecological traits would likely have an impact on the toxin repertoire, which, in the case of B. jararaca species, would enable the species to deal with different prey types during its lifespan.
2016-09-28 | PXD004186 | Pride
Project description:Larvae of the genus Megalopyge (Lepidoptera: Zygaenoidea: Megalopygidae), called asp or puss caterpillars, produce defensive venoms that cause severe acute pain. Here, we present the anatomy, chemistry, and mode of action of the venom systems of caterpillars of two megalopygid species, the Southern flannel moth Megalopyge opercularis and the black-waved flannel moth Megalopyge crispata. We show that megalopygid venom is produced in secretory cells that lie beneath the cuticle and are connected to the venom spines by canals. Megalopygid venoms consist of larger aerolysin-like pore-forming toxins, which we have named megalysins, and a small number of peptides. Venom potently activates mammalian sensory neurons via membrane permeabilization and causes sustained spontaneous pain behaviours and paw swelling in mice. These bioactivities can be easily ablated by treatment with heat, organic solvents, or proteases, suggesting they are mediated by larger proteins, most likely the megalysins. We show that the megalysins were recruited as venom toxins in the Megalopygidae following horizontal transfer of genes from bacteria to the ancestors of Lepidoptera. The megalopygid venom system differs markedly from those of previously studied venomous zygaenoids of the family Limacodidae, suggestive of independent origins. Megalopygids have recruited aerolysin-like proteins as venom toxins convergently with centipedes, cnidarians, and fish. This study highlights the role of horizontal gene transfer in venom evolution.
2024-01-26 | PXD037610 | Pride
Project description:Comprehensive understanding of venom compositions and in-depth characterisation of the various proteoforms are necessary to aid the development of targeted antivenom strategies. This work utilises an integrated 'omics' and intact mass spectrometry-based approach to profile the diversity within the venom of the forest cobra.
2024-01-03 | PXD045209 | Pride
Project description:Combined transcriptomics-assisted bottom-up and top-down MS characterization of the venom proteome of the desert black cobra Walterinnesia aegyptia from Riyadh, SA
2022-02-17 | PXD027498 | Pride
Project description:Combined transcriptomics-assisted bottom-up and top-down MS characterization of the venom proteome of the desert black cobra Walterinnesia morgani from Çörten village, Turkey
2022-02-17 | PXD027497 | Pride