Dataset Information

Coral proteomics study - Combined transcriptomic and proteomic analysis reveals a diversity of venom-related and toxin-like peptides expressed in the mat anemone Zoanthus natalensis (Cnidaria, Hexacorallia)

ABSTRACT: Venoms from marine animals have been recognized as a new emerging source of peptide-based therapeutics. Several peptide toxins from sea anemone have been investigated as therapeutic leads or pharmacological tools. Venom complexity should be further confirmed using novel strategies of large-scale sequencing which integrated transcriptomics and proteomics to provide new putative proteins or peptides to be compared among species. We applied transcriptomic combining with proteomic analyses and identified six groups of peptide toxins including neurotoxin, hemostatic and hemorrhagic toxin, protease inhibitor, mixed function enzymes, venom auxiliary proteins, and peptides related to allergen and innate immunity.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Zoanthus Sp.

TISSUE(S): Whole Body

SUBMITTER: Qiwen Liao

LAB HEAD: Simon Ming-Yuen Lee

PROVIDER: PXD010839 | Pride | 2019-06-24

REPOSITORIES: Pride

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Combined transcriptomic and proteomic analysis reveals a diversity of venom-related and toxin-like peptides expressed in the mat anemone Zoanthus natalensis (Cnidaria, Hexacorallia).

Liao Qiwen Q Gong Guiyi G Poon Terence C W TCW Ang Irene L IL Lei Kate M K KMK Siu Shirley Weng In SWI Wong Clarence Tsun Ting CTT Rádis-Baptista Gandhi G Lee Simon Ming-Yuen SM

Archives of toxicology 20190615 6

Venoms from marine animals have been recognized as a new emerging source of peptide-based therapeutics. Several peptide toxins from sea anemone have been investigated as therapeutic leads or pharmacological tools. Venom complexity should be further highlighted using combined strategies of large-scale sequencing and data analysis which integrated transcriptomics and proteomics to elucidate new proteins or peptides to be compared among species. In this work, transcriptomic and proteomic analyses w ...[more]

PMID: 31203412

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Project description:This study provides comprehensive proteomic profiles from the venom producing posterior salivary glands of Octopus (superorder Octopodiformes) species. A combined transcriptomic and proteomic approach was used to identify 1,703 proteins from the posterior salivary gland of the southern blue ring octopus, Hapalochlaena maculosa and 1,300 proteins from the posterior salivary gland of the southern sand octopus, Octopus kaurna. The two proteomes were broadly similar, clustering of proteins into orthogroups revealed 1,563 of 2,466 clusters were shared between species. Serine proteases were particularly diverse and abundant in both species. Other abundant proteins included a large number of secreted proteins many of which had no known conserved domains, or homology to proteins with known function. Based on homology to known venom proteins, 23 putative toxins were identified in H. maculosa and 24 in O. kaurna. These toxins span nine protein families: CAP (cysteine rich secretory proteins, antigen 5, parthenogenesis related), chitinase, carboxylesterase, DNase, hyaluronidase, metalloprotease, phospholipase, serine protease and tachykinin. Serine proteases were responsible for 70.9% and 86.3% of putative toxin expression in H. maculosa and O. kaurna respectively as determined using intensity based absolute quantification measurements. Phylogenetic analysis of the putative toxin serine proteases revealed a similar suite of diverse proteins present in both species. Venom composition H. maculosa and O. kaurna differ in several key aspects. While O. kaurna expressed the proteinaceous neurotoxin, tachykinin, this was absent from H. maculosa, perhaps reflecting the acquisition of a potent non-proteinaceous neurotoxin, tetrodotoxin (TTX) produced by bacteria in the salivary glands of that species. Dispersal factors particularly hyaluronidase, were disproportionately high in H. maculosa. Chitinase was abundant in both species and is believed to facilitate envenomation in chitinous/crustacean prey. Cephalopods represent a largely unexplored source of novel proteins distinct from all other venomous taxa and are of interest for further inquiry as novel proteinaceous toxins derived from venoms may contribute to pharmaceutical design.

Project description:Assassin bugs (Hemiptera: Heteroptera: Reduviidae) are venomous insects that prey on invertebrates. Assassin bug venom has features in common with venoms from other animals, such as paralysing and lethal activity when injected, and a molecular composition that includes disulfide-rich peptide neurotoxins. Uniquely, this venom also has strong liquefying activity that has been hypothesised to facilitate feeding through the narrow channel of the proboscis—a structure inherited from sap- and phloem-feeding phytophagous hemipterans and adapted during the evolution of Heteroptera into a fang and feeding structure. However, further understanding of the function of assassin bug venom is impeded by the lack of proteomic studies detailing its molecular composition. In addition, the lack of knowledge regarding venoms of predaceous reduviids limits our understanding of how the venoms of the blood-feeding kissing bugs (Reduviidae: Triatominae) evolved to facilitate hematophagy. By using a combined transcriptomic/proteomic approach we show that the venom proteome of the harpactorine assassin bug Pristhesancus plagipennis includes a complex suite of >100 proteins comprising disulfide-rich peptides, CUB-domain proteins, cystatins, putative cytolytic toxins, triabin-like protein, odorant binding protein, serine proteases, catabolic enzymes, putative nutrient-binding proteins, plus eight families of proteins without homology to characterised proteins. Serine proteases, CUB domain proteins and other novel proteins in the 10–16 kDa mass range, as well as putative cytolytic toxins, were the most abundant venom components. Thus, in addition to putative neurotoxins, assassin bug venom includes a high proportion of enzymatic and cytolytic venom components well suited to tissue liquefaction. While some protein families such as lipocalin/triabins occur in the venoms of both predaceous and blood-feeding reduviids, the composition of venoms in these two groups differs markedly. These results provide insights into the venom evolution in the insect suborder Heteroptera.

Dataset Information

Coral proteomics study - Combined transcriptomic and proteomic analysis reveals a diversity of venom-related and toxin-like peptides expressed in the mat anemone Zoanthus natalensis (Cnidaria, Hexacorallia)

Publications

Combined transcriptomic and proteomic analysis reveals a diversity of venom-related and toxin-like peptides expressed in the mat anemone Zoanthus natalensis (Cnidaria, Hexacorallia).

Similar Datasets

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