Halictus scabiosae venom proteome
Ontology highlight
ABSTRACT:
INSTRUMENT(S):
ORGANISM(S): Halictus Scabiosae
TISSUE(S): Venom Gland
SUBMITTER: 
Günter Lochnit
LAB HEAD: Günter Lochnit
PROVIDER: PXD026642 | Pride | 2023-09-28
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| 20201105Biene01.msf | Msf | |||
| 20201105Biene01.mzML | Mzml | |||
| 20201105Biene01.mzid.gz | Mzid | |||
| 20201105Biene01.raw | Raw | |||
| checksum.txt | Txt |
Items per page: 5 1 - 5 of 5 |
Similar Datasets
Project description:In order to provide a global insight on the transcripts expressed in the venom gland of the Brazilian ant species Tetramorium bicarinatum and to unveil the potential of its products, high-throughput expressed sequence tags were generated using Illumina paired-end sequencing technology. A total of 212,371,758 pairs of quality-filtered, 100-base-pair Illumina reads were obtained. The de novo assemblies yielded 36,042 contigs for which 27,873 have at least one predicted ORF among which 59.77% produce significant hits in the available databases. The investigation of the reads mapping toxin class revealed a high diversification with the major part consistent with the classical hymenopteran venom protein signature represented by venom allergen (33.3%) followed by a diverse toxin-expression profile including several distinct isoforms of phospholipase A1 and A2, venom serine protease, hyaluronidase, protease inhibitor and secapin. Moreover, our results revealed for the first time the presence of toxin-like peptides that have been previously identified from unrelated venomous animals such as waprin-like (snakes) and agatoxins (spiders and conus). 300 ant specimens from the species Tetramorium bicarinatum were dissected in order to extract the RNA from their venom gland, The whole ant body was used as a reference,
2015-01-08 | E-GEOD-53988 | biostudies-arrayexpress
Project description:Neuropteran larvae are fierce predators that use venom to feed on arthropods, but their venom system is poorly understood. The iconic antlions (Myrmeleontidae) are adapted to dry, sandy habitats, where they use pitfall traps and venom to catch and subdue large arthropod prey. The aphid lions, larvae of green lacewings (Chrysopidae) primarily hunt for smaller prey, such as aphids. Here, we investigate the tissue origin, composition and ecological role of venom in the European antlion Euroleon nostras and the green lacewing Chrysoperla carnea. We show that E. nostras venom has potent insecticidal activity, indicating its importance for efficient immobilization of large prey. C. carnea venom exerted no toxic effects, reflecting their specialization to small, non-defensive prey. Histological and proteotranscriptomic analysis revealed that antlion venom is produced in three distinct glands that secrete different proteins, indicating a functional compartmentalization of venom compounds. The venom system of E. nostras contains no bacteria, providing strong evidence that all venom compounds are of insect origin and not produced by bacterial symbionts as previously suggested. Our study provides a detailed analysis of the neuropteran venom system and new insights into venom biochemistry and function that may underpin the adaptation of antlions to their unique ecological niche.
2024-08-13 | PXD047026 | Pride
Project description:While the unique symbiotic relationship between anemonefish and sea anemones is iconic, it is still not fully understood how anemonefish withstand and thrive within this venomous host environment. In this study we used a proteotranscriptomics approach to elucidate the proteinaceous toxin repertoire from the most popular host sea anemone Entacmaea quadricolor. Although 1251 different toxin or toxin-like RNA transcripts were expressed in E.quadricolor tentacles and 2736 proteins were detected in milked venom, only 135 (approx. 10%) of proteins in venom were classified as putative toxins. This work raises the perils of defining a dominant venom type based on transcriptomics data alone in sea anemones, as we found that the dominant venom type differed between the transcriptome and proteome data. Moreover, anemonefishes interact with sea anemone proteins, so it is important when determining the dominant toxin type to examine the peptides and proteins that are present in host sea anemone venom and mucus which anemonefishes are known to interact.
2024-01-24 | PXD048736 | Pride
Project description:Animal venoms are a rich source of novel biomolecules with tremendous potential in medicine and agriculture. Ants represent one of the most species-rich lineages of venomous animals. However, only a fraction of their biodiversity has been studied so far. Here, we investigated the venom compositions from Myrmica rubra and Myrmica ruginodis, two members of the Myrmicinae subfamily of ants. We applied a proteo-transcriptomics based venomics workflow. Our analysis revealed that venoms of both species are composed of several protein classes, such as venom serine protease, cysteine-rich secretory proteins, antigen 5 and pathogenesis-related 1 proteins (CAP), Kunitz-type serine protease inhibitors or venom acid phosphatase. Several protein classes identified are known venom allergens, and for the first time we detected phospholipase A1 in the venom of M. ruginodis. We also identified two novel toxins of the epidermal growth factor (EGF) family in its venom proteome and an array of additional EGF-like toxins in venom gland transcriptomes of both species. They display similarity to known toxins from the related myrmecine Manica rubida and the Australian red bulldog ant Myrmecia gullosa of the Myrmeciinae subfamily and may serve as nociceptive weapons in defensive scenarios. Our work suggests that the venoms of M. rubra and M. ruginodis contain many high molecular proteins and enzymes with putatively cell damaging functions. Nevertheless, the presence of EGF-like toxins underpins that myrmicine ants also recruited smaller peptide components into their venom arsenal. Although little is known about the bioactivity and function of these EGF-like toxins, their presence in Myrmecinae and Myrmeciinae suggests that they play an important role for the venom systems of Formicoidea. Our work adds to the emerging picture of ant venoms as a source for novel biomolecules. This underlines the importance to incorporate such taxa in future venom bioprospecting programs.
2022-06-09 | PXD033537 | 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:In the present study, the venom peptidome of the red ant, Manica rubida, was characterized using an integrated transcriptomic and proteomic approach. In addition, insecticidal assays on C18 reversed-phase HPLC venom fractions were conducted on Lucilia caesar blowflies to identify neurotoxic peptides.
2020-03-20 | PXD015675 | Pride
Project description:Heloderma horridum horridum commonly known as the scorpion lizard, Mexican scorpion, and beaded lizard, is a venomous reptile native of America. The venom derived from this lizard has potential applications, particularly in treatment of type II diabetes through the peptide Exendin. In this work, H. h. horridum venom was extracted from adult specimens and lyophilized. To characterize the venom, enzymatic assays, including hyaluronidase, phospholipase A2, and proteolytic activity were conducted. A proteomic analysis of the venom was also performed employing bottom-up/shotgun approaches from SDS-PAGE and High pH Reversed-Phase chromatography., besides fractionation of tryptic peptides using a nano-LC-MS/MS. These approaches involved massive sequencing to enhancing the likelihood of detecting an extensive range of venom proteins. The proteins and peptides found in H. h. horridum venom are reviewed according to the classification of the transcriptome previously reported.
2024-08-10 | PXD052417 | Pride
Project description:Characterizing whole proteins by top-down proteomics avoids a step of inference encountered in the dominant bottom-up methodology when peptides are assembled computationally into proteins for identification. The direct interrogation of whole proteins and protein complexes from the venom of Ophiophagus hannah (king cobra) provides a sharply clarified view of toxin sequence variation, transit peptide cleavage sites and post-translational modifications (PTMs) likely critical for venom lethality. A tube-gel format for electrophoresis (called GELFrEE) and solution isoelectric focusing were used for protein fractionation prior to LC-MS/MS analysis resulting in 131 protein identifications (18 more than bottom-up) and a total of 184 proteoforms characterized from 14 protein toxin families. Operating both GELFrEE and mass spectrometry to preserve non-covalent interactions generated detailed information about two of the largest venom glycoprotein complexes: the homodimeric L-amino acid oxidase (LAAO, ~130 kDa) and the multi-chain toxin cobra venom factor (~147 kDa). The LAAO complex exhibited two clusters of multi-proteoform complexes corresponding to the presence of 5 or 6 N-glycans moieties, each consistent with a distribution of N-acetyl hexosamines. Employing top-down proteomics in both native and denaturing modes provides unprecedented characterization of venom proteoforms and their complexes. A precise molecular inventory of venom proteins will propel the study of snake toxin variation and the targeted development of new anti-venoms or other biotherapeutics.
2016-05-18 | PXD003403 | Pride
Project description:Both single cell and bulk RNA sequencing was performed on expanding or differentiating snake venom gland organoids (from Aspidelaps Lubricus Cowlesi and Naja Nivea), or tissue (Aspidelaps Lubricus Cowlesi). Bulk RNA sequencing from the snake venom gland, liver and pancreas was performed to construct a de novo transcriptome using Trinity.
2020-02-24 | GSE129581 | GEO
Project description:Characterization of the venom proteome of the emerald jewel wasp, Ampulex compressa
2019-01-07 | PXD006340 | Pride