Characterising Functional Venom Profiles of Anthozoans and Medusozoans within Their Ecological Context

Ashwood, Lauren M.; Norton, Raymond S.; Undheim, Eivind A. B.; Hurwood, David A.; Prentis, Peter J.

doi:10.3390/md18040202

Cited by 32 publications

(51 citation statements)

References 142 publications

(213 reference statements)

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“…The venom of medically relevant species, such as the Portuguese Man-o-War ( Physalia physalis ) [ 16 , 17 , 18 ] and several species of box jellyfish ([ 19 , 20 , 21 , 22 ], reviewed in [ 23 ]), or easy to collect species, such as sea anemones [ 24 , 25 ], have been explored more extensively at a biochemical and pharmacological level [ 26 ]. However, these species represent a small fraction of the species diversity within the group, and only recently has the exploration of the venom composition for a wider number of cnidarians increased in an effort to characterize the evolution and ecological function of toxins within the group [ 27 ].…”

Section: Introductionmentioning

confidence: 99%

“…Of the 7142 animal toxins and venoms listed in Tox-Prot, a curated animal venom annotation database, only 273 are derived from cnidarians (as of May 2020, [ 57 ]), with a vast majority (>96%) from anthozoans. Within that limited number there is even greater taxonomic bias; almost 90% of anthozoan toxins are from the Actinioidea superfamily of sea anemones [ 27 , 30 ], meaning less than 50 taxa out of 1100 known sea anemone species contribute to the database of annotated cnidarian toxins [ 54 ]. This taxon bias limits researchers’ ability to discover novel therapeutic peptides and scaffolds from sea anemones, as well as limits to search for potential drug candidates in other anthozoan groups such as corals [ 58 ] and zoanthids [ 47 , 48 , 49 ].…”

Section: Introductionmentioning

confidence: 99%

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Transcriptomic Analysis of Four Cerianthid (Cnidaria, Ceriantharia) Venoms

et al. 2020

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Tube anemones, or cerianthids, are a phylogenetically informative group of cnidarians with complex life histories, including a pelagic larval stage and tube-dwelling adult stage, both known to utilize venom in stinging-cell rich tentacles. Cnidarians are an entirely venomous group that utilize their proteinaceous-dominated toxins to capture prey and defend against predators, in addition to several other ecological functions, including intraspecific interactions. At present there are no studies describing the venom for any species within cerianthids. Given their unique development, ecology, and distinct phylogenetic-placement within Cnidaria, our objective is to evaluate the venom-like gene diversity of four species of cerianthids from newly collected transcriptomic data. We identified 525 venom-like genes between all four species. The venom-gene profile for each species was dominated by enzymatic protein and peptide families, which is consistent with previous findings in other cnidarian venoms. However, we found few toxins that are typical of sea anemones and corals, and furthermore, three of the four species express toxin-like genes closely related to potent pore-forming toxins in box jellyfish. Our study is the first to provide a survey of the putative venom composition of cerianthids and contributes to our general understanding of the diversity of cnidarian toxins.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Transcriptomic Analysis of Four Cerianthid (Cnidaria, Ceriantharia) Venoms

et al. 2020

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“…The venom of medically relevant species, such as the Portuguese Man-o-War (Physalia physalis) [16][17][18] and several species of box jellyfish ( [19][20][21][22], reviewed in [23]), or easy to collect species, such as sea anemones [24,25], have been explored more extensively at a biochemical and pharmacological level [26]. However, these species represent a small fraction of the species diversity within the group, and only recently has the exploration the venom composition for a wider number of cnidarians increased in an effort to characterize the evolution and ecological function of toxins within the group [27].…”

Section: Introductionmentioning

confidence: 99%

“…Of the 7,142 animal toxins and venoms listed in Tox-Prot, a curated animal venom annotation database, only 273 are derived from cnidarians (as of May 2020, [57]), with that vast majority (>96%) are from anthozoans. Within that limited number there is even greater taxonomic bias; almost 90% of anthozoan toxins are from the Actinioidea superfamily of sea anemones [27,30], meaning less than 50 out of 1,100 known sea anemone species contribute to the database of annotated cnidarian toxins [54]. This taxon bias limits researcher's ability to discover novel therapeutic peptides and scaffolds from sea anemones, as well as limits to search for potential drug candidates in other anthozoan groups such as corals [58] and zoanthids [47][48][49].…”

Section: Introductionmentioning

confidence: 99%

“…There is a general consensus that the composition and function of toxins reflects the ecological utility of that venom[133], thus, the increased time in the pelagic environment in the larval stage likely exposes cerianthids to different sets of potential predators and prey, resulting in different selection pressures driving venom composition and function. We can only speculate on the role of these various venom components and overall venom function in the ecological interactions of these animals until additional molecular studies are completed[27,134].One interesting outcome is the difference in the number of venom-like putative protein coding transcripts found in I. nocturnus compared to the other three species(69 compared to 169, 182, 105). As this species is the only representative of the family Arachnactidae, this may be evidence of evolutionary difference compared to the family Cerianthidae, which is corroborated by morphology and traditionally accepted[73].…”

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Transcriptomic analysis of four cerianthid (Cnidaria, Ceriantharia) venoms

Klompen

Macrander

Reitzel

et al. 2020

Preprint

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Tube anemones, or cerianthids, are a phylogenetically informative group of cnidarians 14 with complex life histories, including a pelagic larval stage and tube-dwelling adult stage, both 15 known to utilize venom in stinging-cell rich tentacles. Cnidarians are an entirely venomous group 16 that utilize their proteinaceous-dominated toxins to capture prey and defend against predators, in 17 addition to several other ecological functions, including intraspecific interactions. At present there 18are no studies describing the venom for any species within cerianthids. Given their unique 19 development, ecology, and distinct phylogenetic-placement within Cnidaria, our objective is to 20 evaluate the venom-like gene diversity of four species of cerianthids from newly collected 21 transcriptomic data. We identified 525 venom-like genes between all four species. The venom-gene 22 profile for each species was dominated by enzymatic protein and peptide families, which is 23 consistent with previous findings in other cnidarian venoms. However, we found few toxins that 24 are typical of sea anemones and corals, and furthermore, three of the four species express toxin-like 25 genes closely related to potent pore-forming toxins in box jellyfish. Our study is the first to provide 26 a survey of the putative venom composition of cerianthids, and contributes to our general 27 understanding of the diversity of cnidarian toxins. 28 29 30 1. Introduction 31The phylum Cnidaria (sea anemones, corals, jellyfish, box jellies, hydroids/hydromedusae, 32 etc.) is the earliest diverging venomous lineage (~ 600 million years) [1,2]. Cnidaria deliver their 33 proteinaceous-dominant venom through organelles called nematocysts (a type of cnidae), housed in 34 cells called nematocytes [3,4]. Venom from discharged nematocysts is used in prey capture and 35 defense against predation, but cnidarians also use venom for a variety of other behaviors, such as 36 intraspecific competition [5][6][7] and maternal care [8] (see review by [9]). This ecological diversity is 37 complemented by the functional diversity of cnidarian venoms, which can include neurotoxic, 38 cytotoxic, and enzymatic (e.g. phospholipase and metalloprotease) proteins and peptides, in 39 addition to non-peptidic components [10,11]. For humans, stings from certain species can cause 40 intense localized pain, scarring, induced anaphylaxis, and in the worst cases, cardiac and 41 respiratory failure leading to death [12][13][14][15]. The venom of medically relevant species, such as the 42 Portuguese Man-o-War (Physalia physalis) [16][17][18] and several species of box jellyfish ([19-22], 43 reviewed in [23]), or easy to collect species, such as sea anemones [24,25], have been explored more 44 extensively at a biochemical and pharmacological level [26]. However, these species represent a 45 small fraction of the species diversity within the group, and only recently has the exploration the 46 2 venom composition for a wider number of cnidarians increased in an effort to characterize the 4...

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Structure–function relationships in ShKT domain peptides: ShKT‐Ts1 from the sea anemone Telmatactis stephensoni

Sanches,

Ashwood,

Olushola‐Siedoks

et al. 2023

Proteins

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Diverse structural scaffolds have been described in peptides from sea anemones, with the ShKT domain being a common scaffold first identified in ShK toxin from Stichodactyla helianthus. ShK is a potent blocker of voltage‐gated potassium channels (KV1.x), and an analog, ShK‐186 (dalazatide), has completed Phase 1 clinical trials in plaque psoriasis. The ShKT domain has been found in numerous other species, but only a tiny fraction of ShKT domains has been characterized functionally. Despite adopting the canonical ShK fold, some ShKT peptides from sea anemones inhibit KV1.x, while others do not. Mutagenesis studies have shown that a Lys–Tyr (KY) dyad plays a key role in KV1.x blockade, although a cationic residue followed by a hydrophobic residue may also suffice. Nevertheless, ShKT peptides displaying an ShK‐like fold and containing a KY dyad do not necessarily block potassium channels, so additional criteria are needed to determine whether new ShKT peptides might show activity against potassium channels. In this study, we used a combination of NMR and molecular dynamics (MD) simulations to assess the potential activity of a new ShKT peptide. We determined the structure of ShKT‐Ts1, from the sea anemone Telmatactis stephensoni, examined its tissue localization, and investigated its activity against a range of ion channels. As ShKT‐Ts1 showed no activity against KV1.x channels, we used MD simulations to investigate whether solvent exposure of the dyad residues may be informative in rationalizing and potentially predicting the ability of ShKT peptides to block KV1.x channels. We show that either a buried dyad that does not become exposed during MD simulations, or a partially exposed dyad that becomes buried during MD simulations, correlates with weak or absent activity against KV1.x channels. Therefore, structure determination coupled with MD simulations, may be used to predict whether new sequences belonging to the ShKT family may act as potassium channel blockers.

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Characterising Functional Venom Profiles of Anthozoans and Medusozoans within Their Ecological Context

Cited by 32 publications

References 142 publications

Transcriptomic Analysis of Four Cerianthid (Cnidaria, Ceriantharia) Venoms

Transcriptomic Analysis of Four Cerianthid (Cnidaria, Ceriantharia) Venoms

Transcriptomic analysis of four cerianthid (Cnidaria, Ceriantharia) venoms

Structure–function relationships in ShKT domain peptides: ShKT‐Ts1 from the sea anemone Telmatactis stephensoni

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