Journal ArticleDOI
Equinatoxins, pore-forming proteins from the sea anemone Actinia equina, belong to a multigene family.
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TLDR
The cDNA sequence of a new, sphingomyelin inhibited equinatoxin, EqtIV, is reported, confirming two isoforms of EqtI, differing at position 13, indicating that Eqts belong to a multigene family.About:
This article is published in Toxicon.The article was published on 1999-10-01. It has received 75 citations till now. The article focuses on the topics: Actinia & Stichodactyla helianthus.read more
Citations
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Journal ArticleDOI
Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria).
Gregor Anderluh,Peter Maček +1 more
TL;DR: The crystal structure of equinatoxin II has been determined at 1.9A resolution, and biological, structure-function, and pharmacological characteristics of these cytolysins are reviewed.
Journal ArticleDOI
Sea Anemone (Cnidaria, Anthozoa, Actiniaria) Toxins: An Overview
TL;DR: The phylogentic relationships of sea anemone toxins are assessed, characterized such toxins, the genes encoding them and the toxins three-dimensional structures are characterized, further providing a state-of-the-art description of the procedures involved in the isolation and purification of bioactive toxins.
Journal ArticleDOI
Effects of lipid composition on membrane permeabilization by sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus.
Carlos Álvarez Valcárcel,Mauro Dalla Serra,Cristina Potrich,Ivonne Bernhart,Mayra Tejuca,Diana Martinez,Fabiola Pazos,María E. Lanio,Gianfranco Menestrina +8 more
TL;DR: It is suggested that the insertion of the toxin channel could imply the formation in the bilayer of a nonlamellar structure, a toroidal lipid pore, as in the case of PC/SM mixtures, where permeabilization was optimal when the molar ratio of PA/SM was ~1.
Journal ArticleDOI
Structural basis for self-assembly of a cytolytic pore lined by protein and lipid
TL;DR: The mechanism of action of the haemolytic protein fragaceatoxin C (FraC), a α-barrel PFT, is elucidated by determining the crystal structures of FraC at four different stages of the lytic mechanism, namely the water-soluble state, the monomeric lipid-bound form, an assembly intermediate and the fully assembled transmembrane pore.
Journal ArticleDOI
Evolutionary origin of inhibitor cystine knot peptides
TL;DR: This work has isolated and identified both cDNA and genomic clones for this family of ICK peptides from the scorpion Opistophthalmus carinatus, highlighting a common evolutionary origin for ICK Peptides from animals.
References
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Journal ArticleDOI
Patterns of Amino Acids near Signal‐Sequence Cleavage Sites
TL;DR: In this paper, some such patterns, based on a sample of 78 eukaryotic signal sequences, are presented and discussed, and a first attempt at formulating rules for the prediction of cleavage sites is made.
Journal ArticleDOI
Diversity of Conus neuropeptides
Baldomero M. Olivera,Jean Rivier,Craig Clark,Cecilia A. Ramilo,Gloria P. Corpuz,Fe C. Abogadie,E. Edward Mena,Scott Woodward,David R. Hillyard,Lourdes J. Cruz +9 more
TL;DR: It now seems that the Conus species will each use a distinctive assortment of peptides and that the pharmacological diversity in Conus venoms may be ultimately comparable to that of plant alkaloids or secondary metabolites of microorganisms.
Journal ArticleDOI
Isolation and characterization of three lethal and hemolytic toxins from the sea anemone Actinia equina L.
Peter Maček,Drago Lebez +1 more
TL;DR: Lethal and hemolytic toxins were purified from the tentacles and bodies of the sea anemone Actinia equina and exhibited high lethal potency; the acute i.v. LD50 in mice of equinatoxins I, II and III were 23, 35 and 83 micrograms/kg, respectively.
Journal ArticleDOI
Cloning, Sequencing, and Expression of Equinatoxin II
TL;DR: Recombinant toxin was isolated by a simple, two-step isolation procedure including separation on CM-cellulose and gel filtration using an FPLC system and its biochemical properties and hemolytic activity were practically indistinguishable from those of native toxin.
Journal ArticleDOI
Polypeptide cytolytic toxins from sea anemones (Actiniaria)
TL;DR: Putative biological roles of toxins, based on their channel-forming activity, in the capture and killing of prey, digestion, repelling of predators and intraspecific spatial competition are suggested.
Related Papers (5)
Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria).
Gregor Anderluh,Peter Maček +1 more