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

@article{Kelso1998IdentificationAC,
  title={Identification and characterization of novel sodium channel toxins from the sea anemone Anthopleura xanthogrammica.},
  author={G. Kelso and K. Blumenthal},
  journal={Toxicon : official journal of the International Society on Toxinology},
  year={1998},
  volume={36 1},
  pages={
          41-51
        }
}
  • G. Kelso, K. Blumenthal
  • Published 1998
  • Biology, Medicine
  • Toxicon : official journal of the International Society on Toxinology
Six new toxins from the sea anemone Anthopleura xanthogrammica were identified using a molecular biological approach. Five of these novel isoforms resemble the 47 residue type I long polypeptides native to Anthopleura elegantissima, Anthopleura fuscoviridis and Anemonia sulcata, while one appears to be chimera of the two previously identified 49 residue toxins native to A. xanthogrammica. Four of these toxins were expressed in bacteria, purified and characterized by ion flux assays in RT4-B and… Expand
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A very good correlation exists between the toxic activity to mice, the affinity of the toxin for the Na+ channel in rat brain synaptosomes, and the stimulating effect on 22 Na+ uptake by neuroblastoma cells. Expand
Role of the cationic residues arginine 14 and lysine 48 in the function of the cardiotonic polypeptide anthopleurin B.
TLDR
It is concluded that contrary to results from chemical modification studies, Arg-14 is not essential for the biological activity of the toxin, and Lys-48 plays a small but discernible role in the toxin-receptor interaction. Expand
Cloning and expression of wild-type and mutant forms of the cardiotonic polypeptide anthopleurin B.
TLDR
A synthetic gene for the most toxic of the Anthopleura toxins, anthopleurin B (ApB), has been designed, synthesized, and expressed as a fusion protein with the gene 9 product of bacteriophage T7 in Escherichia coli. Expand
Role for Pro-13 in directing high-affinity binding of anthopleurin B to the voltage-sensitive sodium channel.
TLDR
It is suggested that the P13V mutation results in a shift in the relative orientation of cationic residues within the large flexible loop between residues 9-18, thus strengthening their interactions with target sequences of the neuronal sodium channel. Expand
Importance of highly conserved anionic residues and electrostatic interactions in the activity and structure of the cardiotonic polypeptide anthopleurin B.
TLDR
It is concluded that although a negative charge per se is not essential at position 9, the presence of a hydrogen-bond forming side chain is critical both for appropriate folding and for interaction with the sodium channel. Expand
Importance of the unique cationic residues arginine 12 and lysine 49 in the activity of the cardiotonic polypeptide anthopleurin B.
TLDR
Characterization of three mutants at each of two unique cationic sites of anthopleurin B, Arg-12 and Lys-49 indicate that catedic residues per se are not absolutely required at either position, but that polar side chains at position 12 contribute significantly to binding affinity. Expand
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TLDR
The role of cationic residues is investigated by characterizing toxin mutants in which two such residues are replaced simultaneously, which reduced affinity of the toxin for neuronal channels to a much greater extent than for cardiac channels and produced affinities only slightly lower than for ApA in each case. Expand
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TLDR
The antagonist character of this carboxylate-modified derivative was further confirmed by electrophysiological and Na+ flux experiments and the theoretical and practical significance of these results are discussed. Expand
The Role of Exposed Tryptophan Residues in the Activity of the Cardiotonic Polypeptide Anthopleurin B*
TLDR
Results suggest that a hydrophobic contact is involved in toxin-induced stabilization of the open conformation of the cardiac sodium channel, and W33F is the first ApB mutant that displays a significantly altered association rate and may prove to be a useful probe of the channel binding site. Expand
Amino acid sequence of two sea anemone toxins from Anthopleura fuscoviridis.
TLDR
The amino acid sequences of two toxins from the sea anemone Anthopleura fuscoviridis were determined and have high homology to those of toxins I and II from Anemonia sulcata and anthopleurin-A and -B from anthopleura xanthogrammica. Expand
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