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Leptopilina boulardi (strain Lb17) venom gland proteome

ABSTRACT: The purpose of this project was to identify venom proteins from the venom gland of Leptopilina boulardi (strain Lb17), a parasitoid wasp species that infects fruit flies in the genus Drosophila.

OTHER RELATED OMICS DATASETS IN: PRJNA202370PRJNA202369

INSTRUMENT(S): LTQ XL

ORGANISM(S): Leptopilina Boulardi

TISSUE(S): Venom

SUBMITTER: Todd Schlenke

LAB HEAD: Todd A Schlenke

PROVIDER: PXD023836 | Pride | 2021-01-27

REPOSITORIES: Pride

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			Action	DRS
	checksum.txt	Txt
	jm_20110602_LTQ_Schlenke_Lb17_1.RAW	Raw
	jm_20110602_LTQ_Schlenke_Lb17_1_trin_e_comb2.mzid.gz	Mzid
	jm_20110602_LTQ_Schlenke_Lb17_1_trin_e_comb2.mzid_jm_20110602_LTQ_Schlenke_Lb17_1_trin_e_comb2.MGF	Mzid
	jm_20110602_LTQ_Schlenke_Lb17_2.RAW	Raw

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Publications

Integrative approach reveals composition of endoparasitoid wasp venoms.

Goecks Jeremy J Mortimer Nathan T NT Mobley James A JA Bowersock Gregory J GJ Taylor James J Schlenke Todd A TA

PloS one 20130523 5

The fruit fly Drosophila melanogaster and its endoparasitoid wasps are a developing model system for interactions between host immune responses and parasite virulence mechanisms. In this system, wasps use diverse venom cocktails to suppress the conserved fly cellular encapsulation response. Although numerous genetic tools allow detailed characterization of fly immune genes, lack of wasp genomic information has hindered characterization of the parasite side of the interaction. Here, we use high-t ...[more]

PMID: 23717546

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Leptopilina heterotoma (strain Lh14) venom gland proteome

Project description:The purpose of this project was to identify venom proteins from the venom gland of Leptopilina heterotoma (strain Lh14), a parasitoid wasp species that infects fruit flies in the genus Drosophila.

2021-01-27 | PXD023824 | Pride

Ganaspis hookeri (strain GhFl, formerly 'G1') venom gland proteome

Project description:The purpose of this project was to identify venom proteins from the venom gland of Ganaspis hookeri (strain GhFl, formerly 'G1'), a parasitoid wasp species that infects fruit flies in the genus Drosophila.

2021-01-27 | PXD023825 | Pride

De Novo Transcriptome Sequencing for Tetramorium bicarinatum: The first comprehensive venom gland transcriptome analysis from an ant species.

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

The predatory stink bug Arma chinensis (Hemiptera: Pentatomidae) produces a complex proteinaceous venom to overcome caterpillar prey

Project description:Predatory bugs capture prey by injecting venom from their salivary glands using specialized stylets. Understanding venom function has been impeded by a scarcity of knowledge of their venom composition. We therefore examined the proteinaceous components of the salivary venom of the predatory stink bug Arma chinensis (Hemiptera: Pentatomidae). Using gland extracts and venoms from 5th-instar nymphs or adult females, we performed shotgun proteomics combined with venom gland transcriptomics. We found that the venom of A. chinensis comprised a complex suite of over a hundred individual proteins, including oxidoreductases, transferases, hydrolases, ligases, protease inhibitors, and recognition, transport and binding proteins. Besides the uncharacterized proteins, hydrolases such as venom serine proteases, cathepsins, phospholipase A2, phosphatases, nucleases, alpha-amylases, and chitinases constitute the most abundant protein families. However, salivary proteins shared by and unique to other predatory heteropterans were not detected in A. chinensis venom. Injection of the proteinaceous (> 3 kDa) venom fraction of A. chinensis gland extracts or venom into its prey, the larvae of the Oriental armyworm Mythimna separata (Walker, 1865), revealed insecticidal activity against lepidopterans. Our data expands the knowledge of heteropteran salivary proteins and suggests predatory asopine bugs as a novel source for bioinsecticides.

2023-07-20 | PXD040272 | Pride

Venomics of the Central-European Myrmicine Ants Myrmica rubra and Myrmica ruginodis

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

Exaptation of an evolutionary constraint enables behavioural control over the composition of secreted venom in giant centipedes

Project description:Venoms are biochemical arsenals that have emerged in numerous animal lineages, where they have coevolved with morphological and behavioural traits for venom production and delivery. In centipedes, venom evolution is thought to be constrained by the morphological complexity of their venom glands due to physiological limitations on the number of toxins produced by their secretory cells. Here, we show that the uneven toxin expression that results from these limitations have enabled giant centipedes to regulate the composition of their secreted venom despite having morphologically undifferentiated venom glands. We show that this control is likely achieved by the complex neuronal networks that innervate each venom gland subunit and is facilitated by morphological adaptations that circumvent the physiological evolutionary constraints on venom production. Our results suggest behavioural control over venom composition may be an overlooked aspect of venom biology and provide an example of how exaptation can facilitate evolutionary innovation and novelty.

2024-08-29 | PXD048264 | Pride

Analysis of venom peptide from Conus betulinus

Project description:Characterization of venom peptides from Conus betulinus using mass spectrometry

2023-12-05 | PXD042679 | Pride

Qualitative and quantitative analysis of Bothrops jararaca venom gland proteome

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

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

Physiological constraints dictate toxin spatial heterogeneity in snake venom glands

Project description:Venoms are ecological innovations that have evolved numerous times, on each occasion accompanied by the co-evolution of specialised morphological and behavioural characters for venom production and delivery. The close evolutionary interdependence between these characters is exemplified by animals that control the composition of their secreted venom. This ability depends in part on the production of different toxins in different locations of the venom gland, which was recently documented in venomous snakes. Here, we test the hypothesis that the distinct spatial distributions of toxins in snake venom glands is an adaptation that enables the secretion of venoms with distinct ecological functions.

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