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Discovery of Novel Bilaterian Signaling Peptides Using Cone Snail Toxins

ABSTRACT: Peptide hormones and neuropeptides form a diverse class of signaling molecules that control essential processes in animals. Despite several breakthroughs in peptide discovery, many signaling peptides remain undiscovered. Recently, we demonstrated the use of somatostatin-like toxins from cone snail venom to identify homologous signaling peptides in prey. Here, we demonstrate that this toxin-based approach can be systematically applied to the discovery of other unknown bilaterian signaling peptides. Using large sequencing datasets, we searched for homologies between cone snail toxins and putative peptides from several important model organisms representing the snails’ prey. We identified and confirmed expression of five toxin families that share strong similarities with previously unknown signaling peptides from mollusks and annelids. One of the peptides was also identified in rotifers, brachiopods, platyhelminths, and arthropods, and another was found to be structurally related to crustacean hyperglycemic hormone, a peptide not previously known to exist in Spiralia. Based on several lines of evidence we propose that these signaling peptides not only exist but serve important physiological functions. Finally, we propose that the discovery pipeline developed here can be more broadly applied to other systems in which one organism has evolved molecules to manipulate the physiology of another.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Conus Textile

TISSUE(S): Venom Duct

SUBMITTER: Thomas Koch

LAB HEAD: Helena Safavi-Hemami

PROVIDER: PXD038993 | Pride | 2023-08-18

REPOSITORIES: Pride

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Discovery of Novel Bilaterian Signaling Peptides Using Cone Snail Toxins

Project description:Peptide hormones and neuropeptides form a diverse class of signaling molecules that control essential processes in animals. Despite several breakthroughs in peptide discovery, many signaling peptides remain undiscovered. Recently, we demonstrated the use of somatostatin-like toxins from cone snail venom to identify homologous signaling peptides in prey. Here, we demonstrate that this toxin-based approach can be systematically applied to the discovery of other unknown bilaterian signaling peptides. Using large sequencing datasets, we searched for homologies between cone snail toxins and putative peptides from several important model organisms representing the snails’ prey. We identified and confirmed expression of five toxin families that share strong similarities with previously unknown signaling peptides from mollusks and annelids. One of the peptides was also identified in rotifers, brachiopods, platyhelminths, and arthropods, and another was found to be structurally related to crustacean hyperglycemic hormone, a peptide not previously known to exist in Spiralia. Based on several lines of evidence we propose that these signaling peptides not only exist but serve important physiological functions. Finally, we propose that the discovery pipeline developed here can be more broadly applied to other systems in which one organism has evolved molecules to manipulate the physiology of another.

2023-08-18 | PXD038992 | Pride

Discovery of Novel Bilaterian Signaling Peptides Using Cone Snail Toxins

2023-08-18 | PXD038986 | 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

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

Conus magus venom gland proteomics

Project description:Marine cone snails have attracted researchers from all disciplines but early life stages have received limited attention due to difficulties accessing or rearing juvenile specimens. Here, we document the culture of Conus magus from eggs through metamorphosis to reveal dramatic shifts in predatory feeding behaviour between post-metamorphic juveniles and adult specimens. Adult C. magus capture fish using a set of paralytic venom peptides combined with a hooked radular tooth used to tether envenomed fish. In contrast, early juveniles feed exclusively on polychaete worms using a unique “sting-and-stalk” foraging behaviour facilitated by short, unbarbed radular teeth and a distinct venom repertoire that induces hypoactivity in prey. Our results demonstrate how coordinated morphological, behavioural and molecular changes facilitate the shift from worm- to fish-hunting in C. magus, and showcase juvenile cone snails as a rich and unexplored source of novel venom peptides for ecological, evolutionary and biodiscovery studies.

2023-05-11 | PXD042133 | 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

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

The dual prey-inactivation strategy of spiders - In-depth venomic analysis of Cupiennius salei

Project description:Most knowledge on spider venoms concerns neurotoxins acting on ion channels, whereas proteins and their significance for the envenomation process are neglected. The comprehensive analysis presented here of the venom gland transcriptome and proteome of Cupiennius salei with a focus on proteins and cysteine-containing peptides offers new insight into the structure and function of spider venom, presented here as dual prey-inactivation strategy. After venom injection, many enzymes and proteins, dominated by α-amylase, angiotensin-converting enzyme, and cysteine-rich secretory proteins, interact with main metabolic pathways, leading to major disturbance of the cellular homeostasis. Hyaluronidase and cytolytic peptides destroy tissue and membranes, thus supporting the spread of other venom compounds. We detected 81 transcripts of neurotoxins from 13 peptide families, whereof two families comprise 93.7% of all cysteine-containing peptides. This raises the question of the importance of the other low-expressed peptide families. The identification of a venom gland-specific defensin-like peptide and an aga-toxin-like peptide in the hemocytes offers an important clue on the recruitment and neofunctionalization of body proteins and peptides as the origin of toxins.

2019-03-25 | PXD012881 | 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 dual prey-inactivation strategy of spiders - In-depth venomic analysis of Cupiennius salei

2019-03-25 | PXD012886 | Pride

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