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Stichodactyla haddoni - Proteomic analysis of milked venom

ABSTRACT: To identify proteins present in the milked venom of the sea anemone Stichodactyla haddoni we used a bottom-up proteomics approach to analyze the digested 2DE gel spots, RP-HPLC fractions, as well as crude desalted venom.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Stichodactyla Haddoni

SUBMITTER: Bruno Madio

LAB HEAD: Glenn F. King

PROVIDER: PXD006253 | Pride | 2019-08-13

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20150513_Sha2D_Aa3.group	Other
	20150513_Sha2D_Aa3.wiff	Wiff
	20150513_Sha2D_Aa3.wiff.scan	Wiff
	20150513_Sha2D_Aa3_PeptideSummary.txt	Txt
	20150513_Sha2D_Aa3_ProteinSummary.txt	Txt

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Publications

Parallel Evolution of Complex Centipede Venoms Revealed by Comparative Proteotranscriptomic Analyses.

Jenner Ronald A RA von Reumont Bjoern M BM Campbell Lahcen I LI Undheim Eivind A B EAB

Molecular biology and evolution 20191201 12

Centipedes are among the most ancient groups of venomous predatory arthropods. Extant species belong to five orders, but our understanding of the composition and evolution of centipede venoms is based almost exclusively on one order, Scolopendromorpha. To gain a broader and less biased understanding we performed a comparative proteotranscriptomic analysis of centipede venoms from all five orders, including the first venom profiles for the orders Lithobiomorpha, Craterostigmomorpha, and Geophilom ...[more]

PMID: 31396628

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Calliactis polypus secreted venom

Project description:Venome derived from secreted venom of the sea anemone, Calliactis polypus.Keywords: LC-MSMS, toxin, milked, Cnidaria, Actiniaria

2024-07-13 | PXD045890 | 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

Venoms for all occasions: the functional toxin profiles of different anatomical regions in sea anemones are related to their ecological function

Project description:Phylum Cnidaria is the oldest extant venomous group and is defined by the presence of nematocysts, specialised organelles responsible for venom production and delivery. While nematocysts and toxin peptides are distributed across the entire animal, nematocyst and venom profiles have been shown to differ across morphological structures in actiniarians. In this study, we explore the relationship between patterns of toxin expression and the ecological roles of discrete anatomical structures in Telmatactis stephensoni. Specifically, using a combination of proteomic and transcriptomic approaches, we examined whether there is a direct correlation between the functional similarity of regions and the similarity of their associated toxin expression profiles. We report that the regionalisation of toxin production is consistent with the partitioning of the ecological roles of venom across envenomating structures, and that three major functional regions are present in T. stephensoni— tentacles, epidermis and gastrodermis. Additionally, we find that structures which serve similar functions not only have comparable toxin profiles but also similar nematocyst types. There was no overlap in the toxins identified using proteomics and transcriptomics, however, the expression patterns of specific milked venom peptides were conserved across RNA-seq and mass spectrometry imaging datasets. Furthermore, based on our data, it appears that acontia of T. stephensoni may be transcriptionally inactive and only mature nematocyst are present in the distal portions of the threads. Overall, we find that the venom profile of different anatomical regions in sea anemones varies according to its ecological functions.

2022-05-30 | PXD029717 | Pride

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

Proteomic analysis of Heloderma horridum horridum venom

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

Asp caterpillar (Megalopyge ssp.) venom proteomes

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

Proteotranscriptomics of the most popular hoast sea anemone Entacmaea quadricolor reveals not all toxin genes expressed are recruited into its venom arsenal

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.

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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.

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