Abstract
Naturally occurring toxins can be exquisitely useful chemical tools in neurobiological research. For instance, using an Indian arrow poison extract (curare), the French physiologist Claude Bernard obtained the initial evidence that cells communicate with each other in the nervous system by chemical signals. Also, two potent and highly selective toxins, α-bungarotoxin and tetrodotoxin, served as important chemical tools in first isolating two ion channel membrane proteins, the muscle nicotinic receptor and sodium channel, respectively. A toxin that selectively blocks a particular ion channel can be used to study the physiological and behavioral processes regulated by the channel. Radioisotopically-labeled or fluorescent toxin derivatives can be used to map the distribution of the ion channel, even in different regions within a single cell. In the past decade, these labeled toxins have been extremely valuable probes for identifying new drug leads during high throughput screening of chemical libraries.
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References
Guy, H. R. and Conti, F. (1990) Pursuing the structure and function of voltage-gated channels. Trends Neurosci. 13, 201–206.
Catterall, W. A. (1980) Neurotoxins that act on voltage-sensitive sodium channels in excitable membranes. Ann. Rev. Pharmacol. Toxicol. 20, 15–43.
Goldin, S. (1999) Diversity of mammalian voltage-gated sodium channels. Ann. NYAcad. 868, 38–50.
George, J. D. and George, J. J. (1979) Marine Life: An Illustrated Encyclopedia of Invertebrates in the Sea. John Wiley and Sons, NY, pp. 288.
Tardent, P. (1995) The cnidarian cnidocyte, a high-tech cellular weaponry. BioEssays 17, 351–362.
Watson, G. M. and Hessinger, D. A. (1988) Localization of a purported chemoreceptor involved in triggering cnida discharge in sea anemones, in The Biology of Nematocysts ( Hessinger, D. A. and Lenhoff, H. M., eds.), Academic Press, NY, pp. 255–272.
Cutress, C. E. (1955) An interpretation of the structure and distribution of cnidae in Anthozoa. Syst. Zool. 4, 120–137.
Fautin, D. G. (1988) Importance of nematocysts to Actiniian taxonomy, in Biology of Nematocysts ( Hessinger, D. A. and Lenhoff, H. M., eds.), Academic Press, NY, pp. 487–500.
Kern, W. R. (1988b) Sea anemone toxins: structure and action, in The Biology of Nematocysts ( Hessinger, D. A. and Lenhofff, H. M., eds), Academic Press, NY, pp. 375–405.
Kern, W. R. (1988a) Peptide chain toxins of marine animals, in Biomedical Importance of Marine Organisms, vol. 13 ( Fautin, D., ed.), Calif Acad. Sci., San Francisco, CA pp. 69–83.
Hessinger, D. A., Lenhoff, H. M., and Kahan, L. B. (1973) Haemolytic, phospholipase A and nerve-affecting activities of sea anemone nematocyst venom. Nat. New Biol. 241, 125–127.
Grotendorst, G. R. and Hessinger, D. A. (1999) Purification and partial characterization of the phospholipase A2 and co-lytic factor from sea anemone (Aiptasia pallida) nematocyst venom. Toxicon 37, 1779–1796.
Beress, L., Bruhn, T., Sanchez-Rodriquez, Wachter, E., and Schweitz, H. (2000) Sea anemone toxins acting on Na+-channels and K+-channels: isolation and investigation, in Animal Toxins: Facts and Protocols ( Rochat, H. and Martin-Euclaire, M.-F., eds.), Birkhauser, Basel, pp. 31–56.
Kem, W. R., Parten, B., Pennington, M. W., Dunn, B. M., and Price, D. (1989) Isolation, characterization, and amino acid sequence of a polypeptide neurotoxin occurring in the sea anemone Stichodactyla helianthus. Biochemistry 28, 3483–3489.
Malpezzi, E. L. A., Freitas, J. C., Muramoto, K., and Kamiya, H. (1993) Characterization of peptides in sea anemone venom collected by a novel procedure. Toxicon 31, 853–864.
McKay, M. C. and Anderson, P. A. V. (1988) On the preparation and properties of isolated cnidocytes and cnidae, in The Biology of Nematocysts (Hessinger, D. A. and Lenhoff, H. M., eds.), Academic Press, NY, pp. 273–294
Aneiros, A., Garcia, I., Martinez, J. R., Harvey, A. L., Anderson, A. J., Marshall, D. L., et al. (1993) A potassium channel toxin from the secretion of the sea anemone Bundosoma granulifera. Biochim. Biophys. Acta 1157, 86–92.
Castaneda, O., Sotolongo, V., Amor, A. M., Stocklin, R., Anderson, A. J., Harvey, A. L., et al. (1995) Characterization of a potassium channel toxin from the Caribbean sea anemone Stichodactyla helianthus. Toxicon 33, 603–613.
Spagnuolo, A., Zanetti, L., Cariello, L., and Piccoli, R. (1994) Isolation and characterization of two genes encoding calitoxins, neurotoxic peptides from Calliactis parasitica (Cnidaria). Gene 138, 187–191.
Gendeh, G. S., Chung, M. C. M., and Jeyaseelan, K. (1997a) Genomic structure of a potassium channel toxin from Heteractis magnifica. FEBS Lett. 418, 183–188.
Pennington, M. W., Byrnes, M. E., Zaydenberg, I., Khaytin, I., de Chastonay, J., Krafte, D., et al. (1995) Chemical synthesis and characterization of ShK toxin: a potent potassium channel inhibitor from a sea anemone. Int. J. Pept. Prot. Res. 46, 354–358.
Cotton, J., Crest, M., Bouet, F., Alessandri, N., Gola, M., Forest, E., et al. (1997) A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kvl channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity. Eur. J. Biochem. 244, 192–202.
Gendeh, G. S., Young, L. C., de Medeiros, C. L. C., Jeyaseelan, K., Harvey, A. L., and Chung, M. C. M. (1997) A new potassium channel toxin from the sea anemone Heteractis magnifica: isolation, cDNA cloning, and functional expression. Biochemistry 36, 11, 461–11, 471.
Kelso, G. J. and Blumenthal, K. M. (1998) Identification and characterization of novel sodium channel toxins from the sea anemone Anthopleura xanthogrammica. Toxicon 36, 41–51.
Wunderer, G. (1978): Die Disulfidbrucken von Toxin II aus Anemonia sulcata. HoppeSeyler’s Z. Physiol Chem. 359, 1193–1201.
Beress, L. (1988) Sea anemone toxins as tools for physiological, pharmacological and biophysical research, in Poisonous and Venomous Marine Animals of the World, 2nd ed. ( Halstead, B. W., eds.), Darwin Press, Princeton, pp. 150–161.
Cariello, L., de Santis, A., Fiore, F., Piccoli, R., Spagnuolo, A., Zanetti, L., and Parente, A. (1989) Calitoxin, a neurotoxic peptide from the sea anemone Calliactis paralitica: amino acid sequence and electrophysiological properties. Biochemistry 28, 2484–2489.
Ishida, M., Yokoyama, A., Shimakura, K., Nagashima, Y., and Shiomi, K. (1997) Halcurin, a polypeptide from the sea anemone Halicurias sp., with a structural resemblance to type 1 and type 2 toxins. Toxicon 35, 537–544.
Shiomi, K., Lin, X.-Y., Nagashima, Y., and Ishida, M. (1995) Isolation and amino acid sequence of polypeptide toxins in the sea anemone Condylactis passiflora. Fish. Sci. 61, 1016–1021.
Hellberg, S. and Kem, W. R. (1990) Quantitative structure-activity relationships for sea anemone polypeptide toxins. Int. J. Peptide Prot. Res. 36, 440–444.
Lin, X.-Y., Ishida, M., Nagashima, Y., and Shiomi, K. (1996) A polypeptide toxin in the sea anemone Actinia equina homologous with other sea anemone sodium channel toxins: isolation and amino acid sequence. Toxicon 34, 57–65.
Shiomi, K., Qian, W.-H., Lin, X.-Y., Shimakura, Nagashima, Y., and Ishida, M. (1997) Novel polypeptide toxins with crab lethality from the sea anemone Anemonia erythraea. Biochim. Biophys. Acta.
Loret, E. P., de Valle, R. M., Mansuelle, P., Sampieri, F., and Rochat, H. (1994) Positively charged amino acid residues located similarly in sea anemone and scorpion toxins. J. Biol. Chem. 269, 16,785–16, 788.
Nishida, S., Fujita, S., Warashina, A., Satake, M., and Tamiya, N. (1985) Amino acid sequence of a sea anemone toxin from Parasicyonis actinostoloides. Eur. J. Biochem. 150, 171–173.
Odinokov, S. E., Nabiullin, A. A., Kozlovskaya, E. P., and Elyakov, G. B. (1989) Structure-function relationship of polypeptide toxins: modifying gating mechanism of sodium channel. Pure Appl. Chem. 61, 497–500.
Pallaghy, P. K., Scanlon, M. J., Monks, S. A., and Norton, R. S. (1995) Three-dimensional structure in solution of the polypeptide cardiac stimulant anthopleurin-A. Biochemistry 34, 3782–3794.
Norton, R. S. (1991) Structure and structure-function relationships of sea anemone proteins that interact with the sodium channel. Toxicon 29, 1051–1084.
Monks, S. A., Pallaghy, P. K., Scanlon, M. J., and Norton, R. S. (1995) Solution structure of the cardiostimulant polypeptide anthopleurin-B and comparison with anthpleurin-A. Structure 3, 791–803.
Hinds, M. G. and Norton, R. S. (1993) Sequential H-NMR assingments of neurotoxin HI from the sea anemone Heteractis macrodactylus and structural comparison with related toxins. J Protein Chem. 12, 371–378.
Fogh, E., Kern, W. R., and Norton, R. S. (1990) Solution structure of neurotoxin I from the sea anemone Stichodactylus helianthus. A nuclear magnetic resonance, distance geometry, and restrained molecular dynamics study. J Biol. Chem. 265, 13,016–13, 028.
Wilcox, G. R., Fogh, R. H., and Norton, R. S. (1993) Refined structure in solution of the sea anemone neurotoxin ShI. J. Biol. Chem. 268, 24,707–24, 719.
Scanlon, M. J. and Norton, R. S. (1994) Multiple conformations of the sea anemone polypeptide anthopleurin-A in solution. Prot. Sci. 3, 1121–1124.
Norton, R. S., Cross, K., Braach-Maksvytis, V., and Wachter, E. (1993) 41-n.m.r. study of the solution properties and secondary structure of neurotoxin III from the sea anemone Anemonia sulcata. Biochem. J. 293, 545–551.
Bahraoui, E. M., El Ayab, M., Granier, C., Beress, L., and Rochat, H. (1989) Specificity of antibodies to sea anemone toxin III and immunogenicity of the pharmacological site of anemone and scorpion toxins. Eur. J. Biochem. 180, 55–60.
Pauron, D., Barhanin, J., and Lazdunski, M. (1985) The voltage-dependent Na+ channel of insect nervous system identified by receptor sites for tetrodotoxin, and scorpion and sea anemone toxins. Biochem. Biophys. Res. Comm. 131, 1226–1233.
Schweitz, H., Bidard, J. N., Frelin, C., Pauron, D., Vijverberg, H. P. M., Mahasneh, D. M., and Lazdunski, M. (1985) Purification, sequence, and pharmacological properties of sea anemone toxins from Radianthus paumotensis. A new class of sea anemone toxins acting on the sodium channel. Biochemistry 24, 3554–3561.
Murayama, K. N., Abbott, N. J., Narahashi, T., and Shapiro, B. (1972) Effect of allethrin and Condylactis toxin on the kinetics of sodium conductance of crayfish axon membranes. Comp. Gen. Pharmacol. 3, 391–400.
Bergman, C., DuBois, J. M., Rojas, E., and Rathmayer, W. (1976) Decreased rate of sodium conductance inactivation in the node of Ranvier induced by a polypeptide toxin from sea anemone. Biochim. Biophys. Acta 455, 173–184.
Salgado, V. L. and Kem, W. R. (1992) Actions of three structurally distinct sea anemone toxins on crustacean and insect sodium channels. Toxicon 30, 1365–1381.
El-Sherif, N., Fozzard, H. A., and Hanck, D. A. (1992) Dose-dependent modulation of the cardiac sodium channel by sea anemone toxin ATX II. Circ. Res. 70, 285–301.
Hanck, D. A. and Sheets, M. F. (1995) Modification of inactivation in cardiac sodium channels: ionic current studies with anthopleurin-A toxin. J. Gen. Physiol. 106, 601–616.
Wasserstrom, J. A., Kelly, J. E., and Liberty, K. N. (1993) Modification of cardiac Na+ channels by anthopleurin-A: effects on gating and kinetics. Pflügers Arch. 424, 15–24.
Cannon, S. C. (1996) Sodium channel defects in myotonia and periodic paralysis. Ann. Rev. Neurosci. 19, 141–164.
Cannon, S. C. and Corey, D. P. (1993) Loss of Na+ channel inactivation by anemone toxin (ATX II) mimics the myotonic state in hyperkalaemic periodic paralysis. J. Physiol. 466, 501–520.
Rogers, J. C., Qu, Y., Tanada, T. N., Scheuer, T. and Catterall, W. A. (1996) Molecular determinants of high affinity binding of alpha-scorpion toxin and sea anemone toxin in the S3–S4 extracellular loop in domain IV of the Na+ channel a subunit. J. Biol. Chem. 271, 15,950–15, 962.
Chen, L.-Q., Santarelli, V., Horn, R., and Kallen, R. G. (1996) A unique role for the S4 segment of domain 4 in the inactivation of sodium channels. J. Gen. Physiol. 108, 549–556.
Sheets, M. F. and Hanck, D. A. (1995) Voltage-dependent open-state inactivation of cardiac sodium channels: gating current studies with anthopleurin-A toxin. J. Gen. Physiol. 106, 617–640.
Lawrence, J. C. and Catterall, W. A. (1981) Tetrodotoxin-insensitive sodium channels. Binding of polypeptide neurotoxins in primary cultures of rat muscle cells. J. Biol Chem. 256, 6223–6229.
Scriabine, A., Van Arman, G., Morgan, G., Morris, A. A., Bennett, C. D., and Bohidar, N. R. (1979) Cardiotonic effects of anthopleurin-A, a polypeptide from a sea anemone. J. Cardiovasc. Pharmacol. 1, 571–583.
Catterall, W. A. and Beress, L. (1978) Sea anemone toxin and scorpion toxin share a coinmon receptor site associated with the action potential sodium iontophore. J. Biol. Chem. 253, 7393–7396.
Couraud, F., Rochat, H., and Lissitzky, S. (1978) Binding of scorpion and sea anemone neurotoxins to a common site related to the action potential Na+ ionophore in neuroblastoma cells. Biochem. Biophys. Res. Commun. 83, 1525–1530.
Kem, W. R., Pennington, M. W., Krafte, D. S., and Hill, R. J. (1996a) Sea anemone toxins affecting sodium channels: are the similarities greater than the differences? in Biochemical Aspects of Marine Pharmacology ( Lazarovici, P., Spira, M., and Zlotkin, E., eds.), Alaken Press, Ft. Collins, pp. 98–120.
Benzinger, G. R., Kyle, J. W., Blumenthal, K. M., and Hanck, D. A. (1998) A specific interaction between the cardiac sodium channel and site-3 toxin anthopleurin B. J. Biol. Chem. 273, 80–84.
Kern, W. R., Pennington, M. W., and Dunn, B. M. (1990) Sea anemone polytpeptide toxins affecting sodium channels. Initial structure-activity investigations, in Marine Toxins: Origin, Structure, and Molecular Pharmacology, vol. 418 ( Hall, S., and Strichartz, F., eds.) American Chemical Soc., Washington, DC, pp. 279–289.
Pennington, M. W., Kern, W. R., Norton, R. S., and Dunn, B. M. (1990a) Chemical synthesis of a neurotoxic polypeptide from the sea anemone Stichodactyla helianthus. Intern. J. Pept. Protein Res. 36, 335–343.
Pennington, M. W., Kern, W. R., and Dunn, B. M. (1990) Synthesis and biological activity of six monosubstituted analogs of a sea anemone (Stichodactyla helianthus) type 2 polypeptide toxin. Peptide Res. 3, 1–5.
Mahnir, V. M., Kozlovskaya, E. P., and Elyakov, G. B. (1990) Modification of carboxyl groups in sea anemone toxin RTX-III from Radianthus macrodactylus. Toxicon 28, 1255–1263.
Khera, P. K. and Blumenthal, K. M. (1996) Importance of highly conserved anionic residues and electrostatic interactions in the activity and structure of the cardiotonic polypeptide anthopleurin B. Biochemistry 35, 3503–3507.
Pennington, M. W., Zadenberg, I., Byrnes, M. E., Norton, R. S., and Kern, W. R. (1994) Synthesis of the cardiac inotropic polypeptide anthopleurin-A. J. Pept. Prot. Res. 43, 463–470.
Gallagher, M. J. and Blumenthal, K. M. (1992) Cloning and expression of wild-type and mutant forms of the cardiotonic polypeptide anthopleurin B. J. B.ol. Chem. 267, 13,95813, 963.
Gallagher, M. J. and Blumenthal, K. M. (1994) Importance of the unique cationic residues arginine 12 and lysine 49 in the activity of the cardiotonic polypeptide anthopleurin B. J. Biol. Chem. 269, 254–259.
Khera, P. K. and Blumenthal, K. M. (1994) Role of the cationic residues arginine 14 and lysine 48 in the function of the cardiotonic polypeptide anthopleurin B. J. Biol. Chem. 269, 921–925.
Khera, P. K., Benzinger, F. R., Lipkind, G., Drum, C. L., Hanck, D. A., and Blumenthal, K. M. (1995) Multiple cationic residues of anthopleurin B that determine high affinity and channel isoform discrimination. Biochemistry 34, 8533–8541.
Kelso, G. J., Drum, C. L., Hanck, D. A., and Blumenthal, K. M. (1996) Role for Pro-13 in directing high-affinity binding of anthopleurin B to the voltage-sensitive sodium channel. Biochemistry 35, 14, 157–14, 164.
Dias-Kadambi, B. L., Drum, C. L., Hanck, D. A., and Blumenthal, K. M. (1996) Leucine 18, a hydrophobic residue essential for high affinity binding of anthopleurin B to the voltage-sensitive sodium channel. J. Biol. Chem. 271, 9422–9428.
Fetrow, J. S. (1995) Omega loops: nonregular secondary structures significant in protein function and stability. FASEB J. 9, 708–717.
Benzinger, G. R, Drum, C. L., Chen, L.-Q., Kallen, R. G., and Hanck, D. A. (1997) Differences in the binding sites of two site-3 sodium channel toxins. Pflügers Arch. Eur. J. Physiol. 434, 742–749.
Gould, A. R., Mabbutt, B. C., Llewellyn, L. E., Goss, N. H., and Norton, R. S. (1992) Linear and cyclic peptide analogues of the polypeptide cardiac stimulant, anthopleurin-A. 1HNMR and biological activity studies. Eur. J. Biochem. 206, 641–651.
Renaud, J. F., Fosset, M., Schweitz, H., and Lazdunski, M. (1986) The interaction of polypeptide neurotoxins with tetrodotoxin-resistant Na+ channels in mammalian cardiac cells. Correlation with inotropic and arrhythmic effects. Eur. J. Pharmacol. 120, 161–170.
Blair, R. W., Peterson, D. F., and Bishop, V. S. (1978) The effect of anthopleurin-A on cardiac dynamics in conscious dogs. J. Pharm. Exp. Ther. 207, 271–276.
Norton, R. S. (1997) Polypeptide modulators of sodium channel function as a basis for the development of novel cardiac stimulants, in Structure Based Drug Design ( Veerapandian, P., ed.), Marcel Dekker, NY, pp. 295–319.
Hashimoto, Y. and Ashida, K. (1987) Screening of toxic corals and isolation of a toxic polypeptide from Goniopora spp. Publ. Seto. Mar. Biol. Lab. 20, 703–711.
Ashida, K., Toda, H., Fujiwara, M., and Sakiyama, F. (1987) Amino acid sequence of Goniopora toxin. Jpn. J. Pharmacol. 43(Suppl.)33, (abstract P-33).
Fujiwara, M., Muramatsu, I., Hidaka, H., Ikushima, S., and Ashida, K. (1979) Effects of Goniopora toxin, a polypeptide isolated from coral, on electromechanical properties of rabbit myocardium. J. Pharm. Exp. Ther. 210, 153–157.
Noda, M., Muramatsu, I., and Fujiwara, M. (1984) Effects of Goniopora toxin on the membrane currents of fullfrog atrial muscle. N. S. Arch. Pharmacol. 327, 75–80.
Ikushima, S., Muramatsu, I., Fujiwara, M., and Ashida, K. (1981) Relationship between the effects of Goniopora toxin on action potential and on contractile force in guinea-pig papillary muscle. Jpn. J. Pharmacol. 31, 1051–1060.
Muramatsu, I., Fujiwara, M., Miura, A., and Narahashi, T. (1985) Effects of Goniopora toxin on crayfish giant axons. J. Pharm. Exp. Ther. 234, 307–315.
Gonoi, T., Ashida, K., Feller, D., Schmidt, J., Fujiwara, M., and Catterall, W. A. (1986) Mechanism of action of a polypeptide neurotoxin from the coral Goniopora on sodium channels in mouse neuroblastoma cells. Mol. Pharmacol. 29, 347–354.
Qar, J., Schweitz, H., Schmid, A., and Lazdunski, M. (1986) A polypeptide toxin from the coral Goniopora. Purification and action on Cat+ channels. FEBS Lett. 202, 331–336.
Minagawa, S., Isida, I., Nagashima, Y., and Shiomi, K. (1998) Primary structure of a potassium channel toxin from the sea anemone Actinia equina. FEBS Lett. 427, 149–151.
Harvey, A. L., Rowan, E. G., Vatanpour, H., Young, L. C., Castaneda, O., Mebs, D., et al. (1996) Potassium channel neurotoxins from sea anemones, in Biochemical aspects of Marine Pharmacology ( Lazarovici, P., Spira, M., and Zlotkin, E., eds.), Alaken Press, Ft. Collins, pp. 121–131.
Pohl, J., Hubalek, F., Byrnes, M. E., Nielsen, K. R., Woods, A., and Pennington, M. W. (1995) Assignment of the three disulfide bonds in ShK toxin: a potent potassium channel inhibitor from the sea anemone Stichodactyla helianthus. Lett. Peptide Sci. 1, 291–297.
Kem, W. R., Sanyal, G., Williams, R. W., and Pennington, M. W. (1996b) Secondary structure of ShK toxin, a potassium channel-blocking peptide. Lett. Peptide Sci. 3, 69–72.
Tudor, J. E., Pallaghy, P. K., Pennington, M. W., and Norton, R. S. (1996) Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone. Nature Str. Biol. 3, 317–320.
Lanigan, M. D., Tudor, J. E., Pennington, M. W., and Norton, R. S. (2001) A helical cap- ping motif in ShK toxin and its role in helix stabilization. Biopolymers 58, 422–436.
Dauplais, M., Lecoq, A., Song, J., Cotton, J., Jamin, N., Gilquin, B., et al. (1997) On the convergent evolution of animal toxins. conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J. Biol. Chem. 272, 4302–4309.
Tudor, J. E., Pennington, M. W., and Norton, R. S. (1998) Ionization behaviour and solution properties of the potassium-channel blocker ShK toxin. Eur. J. Biochem. 251, 133–141.
Schweitz, H., Bruhn, T., Guillemare, M. D, Lancelin, J.-M., Beress, L., and Lazdunshi, M. (1995) Kalicludines and Kaliseptine: Two different classes of sea anemone toxins for voltage-sensitive K+ channels. J. Biol. Chem. 270, 25,121–25, 126.
Diochot, S., Schweitz, H., Beress, L., and Lazdunski, M. (1998) Sea anemone peptides with a specific blocking activity against fast inactivating potassium channel Kv3.4. J. Biol. Chem. 73, 6744–6749.
Llewellyn, L. E. and Norton, R. S. (1991) Binding of the sea anemone polypeptide BdS II to the voltage-gated sodium channel. Biochem. Intern. 24, 937–946.
Pennington, M. W., Mahnir, V. M., Krafte, D. S., Zadenberg, I., Byrnes, M. E., Khaytin, I., et al. (1996) Identification of three separate binding sites on ShK toxin, a potent inhibitor of voltage-dependent potassium channels in human T-lymphocytes and rat brain. Biochem. Biophys. Res. Commun. 219, 696–701.
Kalman, K., Pennington, M., Nguyen, A., Mahnir, V. M., Kem, W R., Grissmer, S., et al. (1998) ShK-K22DAP: A potent Kv1.3-specific immunosuppressive peptide. J. Biol. Chem. 273, 32,697–32, 707.
Brugnara, C., Armsby, C. C., De Franceschi, L., Crest, M., Martin Euclaire, M. F., and Alper, S. L. (1995) Ca2tactivated K+ channels of human and rabbit erythrocytes display distinctive patterns of inhibition by venom peptide toxins. J. Memhr. Biol. 147, 71–82.
Rauer, H., Pennington, M. W., Cahalan, M. D., and Chandy, K. G. (1999) Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin. J. Biol. Chem. 274, 21,885–21, 892.
Aiyar, J. (1999) Potassium channels in leukocytes and toxins that block them: structure, function and therapeutic implications. Perspect Drug Disc. Design 15/16, 257–280.
Araque, A., Urbano, F. J., Cervenansky, C., Gandia, L., and Buno, W. (1995) Selective block of Ca’-dependent K+ current in crayfish neuromuscular system and chromaffin cells by sea anemone Bunodosoma cangicum venom. J. Neurosci. Res. 42, 539–546.
Pennington, M. W., Mahnir, V. M., Khaytin, I., Zaydenberg, I, Byrnes, M. E., and Kem, W. R. (1996): An essential binding surface for ShK toxin interaction with rat brain potassium channels. Biochemistry 35, 16, 407–16, 411.
Alessandri-Haber, N., Lecoq, A., Gasparin, S., Grangier-Macmath, G., Jacquet, G., Harvey, A. L., et al. (1999) Mapping the functional anatomy of BgK on Kv1.1, Kvl.2, and Kv1.3. Clues to design analogs with enhanced selectivity. J. Biol. Chem. 274, 35,653–35, 661.
Kem, W. R., Pennington, M. W., and Norton, R. S. (1999) Sea anemone toxins as templates for the design of immunosuppressant drugs. Perspec. Drug Disc. Design 15/16, 111–129.
Pennington, M. W., Mahnir, V. M., Baur, P., McVaugh, C. T., Behm, D., and Kem, W. R. (1997b) The effect of truncation on ShK toxin: elimination of the amino-carboxyl terminal (3–35) disulfide linkage stabilizing the amino and carboxyl terminal segments. Prot. Peptide Lett. 4, 23 7–242.
Pennington, M. W., Lanigan, M. D., Kalman, K., Mahnir, V. M., Rauer, H., McVaugh, C. T., et al. (1999) Role of disulfide bonds in the structure and potassium channel blocking activity of ShK toxin. Biochemistry 38, 14, 549–14, 558.
Tytgat, J., Debont, T., Carmeliet, E., and Daenens, P. (1995) The alpha-dendrotoxin footprint on a mammalian potassium channel. J. Biol. Chem. 270, 24,776–24, 781.
Janin, J. and Chothia, C. (1990) The structure of protein-protein recognition sites. J. Biol. Chem. 265, 16,027–16, 030.
Novotny, J. and Haber, E. (1986) Static accessibility model of protein antigenicity: the case of scorpion neurotoxin. Biochemistry 25, 6748–6754.
Doyle, D. A., Cabral, J. M., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., et al. (1998) The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science 280, 69–77.
MacKinnon, R., Cohen, S. L., Kuo, A., Lee, A., and Chait, B. T. (1998) Structural conservation in prokaryotic and eukaryotic potassium channels. Science 280, 106–109.
Mariscal, R. N. (1970), The nature of the symbiosis between Indo-Pacific anemone fishes and sea anemones. Mar. Biol. 6, 58–65.
Fautin, D. G. (1991), The anemone-fish symbiosis: what is known and what is not. Symbiosis 10, 23–46.
de Couet, H. G. (1982), Coelenterate nematocysts bind immunoglobulins. Experientia 38, 353–354.
Maier, L. and Rathmayer, W. (1982), Lokalisierung von Anemonentoxin in den Tentakeln der Wachsrose Anemonia sulcata (Coelenterata) mit Hilfe spezifischer Antikorper. Verh. Dtsch. Zool. Ges. 281 (Abstr.).
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Kem, W.R. (2002). Anthozoan Neurotoxins. In: Massaro, E.J. (eds) Handbook of Neurotoxicology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-132-9_25
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DOI: https://doi.org/10.1007/978-1-59259-132-9_25
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