Halcurin, a polypeptide toxin from the sea anemone Halcurias sp., with a structural resemblance to type 1 and 2 toxins
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Cited by (27)
The pharmacology of voltage-gated sodium channel activators
2017, NeuropharmacologyCitation Excerpt :Sea anemone toxins that associate with NaV channels are categorised into three groups: Type I, II and III (Frazao et al., 2012; Moran et al., 2009; Norton, 1991). However, in recent years questions about the validity of these broad classifications have arisen as additional peptides are discovered and characterised that diverge from the stringent structural and functional properties proposed originally (Ishida et al., 1997; Moran et al., 2009). Sea anemone toxins bind to site 3 and produce a delay in inactivation at low concentrations as well as a large persistent current at high concentrations (Catterall and Beress, 1978; Moran et al., 2007; Smith and Blumenthal, 2007).
The voltage-gated sodium channel: A major target of marine neurotoxins
2014, ToxiconCitation Excerpt :ATX III structure consists in four reverse turns and two other chain reversals and does not contain regular α-helix or β-sheet structure (Manoleras and Norton, 1994) (Fig. 3). The classification has become more complex since the discovery of novel toxins like halcurin (from Halcurias sp.) which display common feature with type I and type II SaNaTx or more recently AdE-1 (from Aiptasia diaphana) which act on both Nav channels and voltage-gated K+ channels (Ishida et al., 1997; Nesher et al., 2013, 2014). Facing the molecular diversity of SaNaTx, the scientific community has suffered from the lack of a systematic nomenclature, leading to ambiguous situations due to (i) the assignation of multiple names to the same sea anemone toxin and (ii) the same name to toxins from unrelated species.
Isolation and cDNA cloning of type 2 sodium channel peptide toxins from three species of sea anemones (Cryptodendrum adhaesivum, Heterodactyla hemprichii and Thalassianthus aster) belonging to the family Thalassianthidae
2010, Comparative Biochemistry and Physiology - B Biochemistry and Molecular BiologyCitation Excerpt :We recently obtained three species of sea anemones (Cryptodendrum adhaesivum, Heterodactyla hemprichii and Thalassianthus aster) belonging to the family Thalassianthidae and found that their extracts exhibited potent lethality to crabs. It should be noted that all the sea anemones so far examined for toxins are members of the family Actiniidae (e.g. A. elegantissima) or Stichodactylidae (e.g. S. gigantea), except for only two species, Halcurias sp. (Ishida et al., 1997) of the family Halcuriidae and Calliactis parasitica (Cariello et al., 1989; Spagnuolo et al., 1994) of the family Hormathiidae, both of which contain site-3 sodium channel toxins. It is therefore important to clarify what classes of crab-lethal toxins are contained in the three species of Thalassianthidae, especially from the viewpoint of comparative biochemistry.
Sea anemone toxins affecting voltage-gated sodium channels - molecular and evolutionary features
2009, ToxiconCitation Excerpt :Indeed, not only can a variety of toxin configurations be found in their venom (Honma and Shiomi, 2006), but it has been shown that each toxin is encoded by a gene family (Moran et al., 2008a). The toxins active on voltage-gated sodium channels are abundant in all sea anemone venoms assayed to date, and are present even in rare and highly unique species (Ishida et al., 1997; Moran and Gurevitz, 2006). The abundance of these toxins and the fact they constitute a major fraction of the proteinaceous content of the venom (Beress et al., 1975) points to their major role in predation and defense.