Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The venom profile of the solitary European carpenter bee Xylocopa violacea

ABSTRACT: 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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Xylocopa Violacea

TISSUE(S): Venom Gland

SUBMITTER: Bjoern von Reumont

LAB HEAD: Sebastien Dutertre

PROVIDER: PXD030997 | Pride | 2023-06-26

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	VENOMICS_201013_HFX_Xxvio.mgf	Mgf
	VENOMICS_201013_HFX_Xxvio.mzxml	Mzxml
	checksum.txt	Txt
	peptides_1_1_0.mzid.gz	Mzid

Items per page:

1 - 4 of 4

Similar Datasets

Proteomics of the venom from Xylocopa violacea

Project description:Venoms have convergently evolved in all major animal lineages and are ideal candidates to unravel the underlying genomic processes of convergent trait evolution. However, few animal groups have been studied in detail, and large-scale comparative genomic analyses to address toxin gene evolution are rare. Hyper-diverse hymenopterans are the most speciose group of venomous animals, but the origin of their toxin genes have been largely overlooked. We combined proteo-transcriptomics with comparative genomics compiling an up-to-date list of core bee venom proteins to investigate the origin of 11 venom genes in 30 hymenopteran genomes including two new stingless bees.

2022-04-04 | PXD029823 | Pride

Proteomics of the venom from Apis mellifera

2023-09-28 | PXD029934 | Pride

Venomics of the desert black cobra Walterinnesia aegyptia from Riyadh, SA

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

Venomics of the desert black cobra Walterinnesia morgani from Çörten village, Turkey

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

Venomics of the desert black cobra Walterinnesia aegyptia from Sinai Peninsula, Egypt

Project description:Combined transcriptomics-assisted bottom-up and top-down MS characterization of the venom proteome of the desert black cobra Walterinnesia aegyptia from Sinai Peninsula, Egypt.

2022-02-17 | PXD027495 | Pride

Characterization of the gila monster (Heloderma suspectum suspectum) venom proteome

Project description:The archetypical venomous lizard species are the helodermatids, the Gila Monster (Heloderma suspectum) and the Beaded Lizards (Heloderma horridum). In the present study, the gila monster venom proteome was characterized using 2D-gel electrophoresis and tandem mass spectrometry-based de novo peptide sequencing followed by protein identification based on sequence homology. A total of 39 different proteins were identified out of the 58 selected spots that represent the major constituents of venom. Of these proteins, 19 have not previously been identified in helodermatid venom. The data showed that helodermatid venom is complex and that this complexity is caused by genetic isoforms and post-translational modifications including proteolytic processing. In addition, the venom proteome analysis revealed that the major constituents of the gila monster venom are kallikrein-like serine proteinases (EC 3.4.21) and phospholipase A2 (type III) enzymes (EC 3.1.1.4). A neuroendocrine convertase 1 homolog that most likely converts the proforms of the previously identified bioactive exendins into the mature and active forms was identified suggesting that these peptide toxins are secreted as proforms that are activated by proteolytic cleavage following secretion as opposed to being activated intracellularly. The presented global protein identification-analysis provides the first overview of the helodermatid venom composition.

2015-01-26 | PXD001343 | Pride

Venom composition and pain-causing toxins of the Australian great carpenter bee Xylocopa aruana

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.

2023-03-11 | PXD038183 | Pride

Taxon-specific toxicity and composition of venom produced by araneophagous white-tailed spiders (Lamponidae: Lampona sp.)

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

Saddleback caterpillar venom proteomics

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

Venom proteomics of Indonesian king cobra

Project description:Complementary bottom-up MS/MS analyses contributed to complete a locus-resolved venom phenotype map for O. hannah, the world's longest venomous snake and a species of medical concern across its wide distribution range in forests from India through Southeast Asia. Its venom composition convincingly explains the main neurotoxic effects of human envenoming caused by king cobra bite. The integration of efficient chromatographic separation of the venom components, and locus-resolved toxin identification through top-down and bottom-up MS/MS-based species-specific database searching, promises a bright future to the field of venom research.

2015-08-20 | PXD001726 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data