Identification and characterization of novel sodium channel toxins from the sea anemone Anthopleura xanthogrammica

Kelso, Gregory J.; Blumenthal, Kenneth M.

doi:10.1016/s0041-0101(97)00064-0

Cited by 24 publications

(13 citation statements)

References 34 publications

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“…Transcripts for sea anemone toxins were isolated from several species usually mostly via PCR reactions based on and degenerate primers (Spagnuolo et al, 1994; Kelso and Blumenthal, 1998; Anderluh et al, 2000; Honma et al, 2005). As shown for other nematocyst proteins, sea anemone These toxins seem to be translated as precursors, carrying a leader peptide and a propart region, which have been suggested to have a role in intracellular sorting and delivery to the nematocyst (Anderluh et al, 2000).…”

Section: Genomic Organization and Evolution Of Sea Anemone Toxin Genesmentioning

confidence: 99%

Sea anemone toxins affecting voltage-gated sodium channels – molecular and evolutionary features

Moran

Gordon

Gurevitz

2009

Toxicon

101

102

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The venom of sea anemones is rich in low molecular weight proteinaceous neurotoxins that vary greatly in structure, site of action, and phyletic (insect, crustacean or vertebrate) preference. This toxic versatility likely contributes to the ability of these sessile animals to inhabit marine environments co-habited by a variety of mobile predators. Among these toxins, those that show prominent activity at voltage-gated sodium channels and are critical in predation and defense, have been extensively studied for more than three decades. These studies initially focused on the discovery of new toxins, determination of their covalent and folded structures, understanding of their mechanisms of action on different sodium channels, and identification of the primary sites of interaction of the toxins with their channel receptors. The channel binding site for Type I and the structurally unrelated Type III sea anemone toxins was identified as neurotoxin receptor site 3, a site previously shown to be targeted by scorpion alpha-toxins. The bioactive surfaces of toxin representatives from these two sea anemone types have been characterized by mutagenesis. These analyses pointed to heterogeneity of receptor site 3 at various sodium channels. A turning point in evolutionary studies of sea anemone toxins was the recent release of the genome sequence of Nematostella vectensis, which enabled analysis of the genomic organization of the corresponding genes. This analysis demonstrated that Type I toxins in Nematostella and other species are encoded by gene families and suggested that these genes developed by concerted evolution. The current review provides a brief historical description of the discovery and characterization of sea anemone toxins that affect voltage-gated sodium channels and delineates recent advances in the study of their structure-activity relationship and evolution.

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Section: Genomic Organization and Evolution Of Sea Anemone Toxin Genesmentioning

confidence: 99%

Sea anemone toxins affecting voltage-gated sodium channels – molecular and evolutionary features

Moran

Gordon

Gurevitz

2009

Toxicon

101

102

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“…The corresponding three-dimensional representation in Figure 4 results in The sequences were obtained from the following papers: AeI (Actinia equina): [27], AETX I (Anemonia erythraea): [28], APE 1-1, APE 1-2, APE 2-1 (Anthopleura elegantissima): [29], AFT-I, AFT-II (Anthopleura fuscoviridis): [30], ATX-Ia, ATX-I, ATX-II, ATX-V ATX-III, ATX-IV (Anemonia sulcata): [31][32][33][34][35][36], Ap-A, Ap-B, PCR1-2, PCR 2-1, PCR2-5, PCR 2-10, PCR 3-3, PCR 3-6, PCR 3-7 (Anthopleura xanthogrammica): [37][38][39], BcIII (Bunodosoma caissarum): [40], Bg II, Bg III (Bunodosoma granulifera): [41], Cp II (Condylactis passiflora): [42], RTX-I, RTX-II, RTX-III, RTX-IV, RTX-V (Radianthus macrodactylus/previously Heteractis macrodactylus): [43][44][45], RpII, RpIII (Radianthus paumotensis/previously Heteractis magnífica or Heteractis paumotensis): [46][47], Sh I (Stichodactylae helianthus): [48], CLX-I, CLX-II (Calliactis parasitica): [19], Halcurin (Halcurias carlgreni): [49], PA-TX (Parasicyonis actinostoloides/previously Entacmaea quadricolor): [50].…”

Section: Resultsmentioning

confidence: 99%

Functional discrimination of sea anemone neurotoxins using 3D-plotting

et al. 2009

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Abstract:One of the most important goals in structural biology is the identification of functional relationships among the structure of proteins and peptides. The purpose of this study was to (1) generate a model based on theoretical and computational considerations among amino acid sequences within select neurotoxin peptides, and (2) compare the relationship these values have to the various toxins tested. We employed isolated neurotoxins from sea anemones with established specific potential to act on voltage-dependent sodium and potassium channel activity as our model. Values were assigned to each amino acid in the peptide sequence of the neurotoxins tested using the Number of Lareo and Acevedo algorithm (NULA). Once the NULA number was obtained, it was then plotted using three dimensional space coordinates. The results of this study allow us to report, for the first time, that there is a different numerical and functional relationship between the sequences of amino acids from sea anemone neurotoxins, and the resulting numerical relationship for each peptide, or NULA number, has a unique location in three-dimensional space.

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“…According to sequence homologies sodium channel toxins can be classified as types I and II [78]: • Type I toxins are represented by ATXI, ATXII and ATXV from A. sulcata, AftI and AftII from Anthopleura fuscoviridis, ApA and ApB from A. xantogrammica, ApC from A. elegantissima [90,92] and BgII and BgIII from Bunodosoma granulifera among others [93,94]. • Type II toxins include ShI from S. helianthus and toxins from Heteractis sp.…”

Section: Channel Toxinsmentioning

confidence: 99%

“…Chemical modification studies of sea anemone toxins were carried out by several laboratories to determine the role of different amino acids in the channel binding but do not exist a general conclusion about the role of each residue, however different residues that seem to play a role in the interaction with toxin receptor such as Arg-12, Arg-14, Lys-49 and Lys-37 were identified [92,100,101]. In general, basic amino acids of toxins and acidic residues of the domains I and IV of the sodium channel alpha subunit have been implicated in toxin binding.…”

Section: Channel Toxinsmentioning

confidence: 99%

Bioactive peptides from marine sources: pharmacological properties and isolation procedures

Aneiros¹,

Garateix²

2004

Journal of Chromatography B

294

180

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Marine organisms represent a valuable source of new compounds. The biodiversity of the marine environment and the associated chemical diversity constitute a practically unlimited resource of new active substances in the field of the development of bioactive products. In this paper, the molecular diversity of different marine peptides is described as well as information about their biological properties and mechanisms of action is provided. Moreover, a short review about isolation procedures of selected bioactive marine peptides is offered. Novel peptides from sponges, ascidians, mollusks, sea anemones and seaweeds are presented in association with their pharmacological properties and obtainment methods.

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Identification and characterization of novel sodium channel toxins from the sea anemone Anthopleura xanthogrammica

Cited by 24 publications

References 34 publications

Sea anemone toxins affecting voltage-gated sodium channels – molecular and evolutionary features

Sea anemone toxins affecting voltage-gated sodium channels – molecular and evolutionary features

Functional discrimination of sea anemone neurotoxins using 3D-plotting

Bioactive peptides from marine sources: pharmacological properties and isolation procedures

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