Venoms neurotoxins from

Neurotoxins from Sea Snake and Other Vertebrate Venoms... 

The similarity of the primary structure of different sea snake venoms has already been discussed. Postsynaptic neurotoxins from Elapidae venom have been extensively studied. Elapidae include well-known snakes such as cobra, krait, mambas, coral snakes, and all Australian snakes. Like sea snake toxins, Elapidae toxins can also be grouped into short-chain (Type I) and long-chain (Type II) toxins. Moreover, two types of neurotoxins are also similar to cardiotoxins, especially in the positions of disulfide bonds. However, amino acid sequences between cardiotoxins and sea snake and Elapidae neurotoxins are quite different. In comparing the sequence of sea snake and Elapidae neurotoxins, there is a considerable conservation in amino acid sequence, but the difference is greater than among the various sea snake toxins. 

Grishin, E. V. (1996). Neurotoxin from black widow spider venom. Structure and function. Advances in Experimental Medicine and Biology 391 231-236. 

Abe T, Alemd S, Miledi R (1977) Isolation and characterization of presynaptically acting neurotoxins from the venom of bungarus snakes. Eur J Biochem 80 1-12... 

Lee CY, Chang CC, Chen YM (1972) Reversibility of neuromuscular blockade by neurotoxins from elapid and sea snake venoms. Taiwan Yi Xue Hui Za Zhi 71 344-9 Lee CY, Tsai MC, Chen YM, Ritonja A, Gubensek F (1984) Mode of neuromuscular blocking action of toxic phospholipases A2 from vipera ammodytes venom. Arch Int Pharmacodyn Ther 268 313-24... 

Pearson JA, Tyler MI, Retson KV, Howden ME (1993) Studies on the subunit structure of tex-tilotoxin, a potent presynaptic neurotoxin from the venom of the australian common brown snake (pseudonaja textilis). 3. the complete amino-acid sequences of all the subunits. Biochem Biophys Acta 1161 223-9... 

Sheumack, D. D., Howden, M. E. H., Spence, I. and Quinn, R. J. 1978. Maculotoxin a neurotoxin from the venom glands of the octopus Hapalochlaena maculosa identified as tetrodotoxin. Science 199, 188-189... 

Long neurotoxin from the venom of the Asian cobra... 

Mixed polypeptide complex neurotoxin from rattlesnake venom. Prevents ACh release and blocks muscle ACh receptor. Systemic effects dizziness, sensory and motor depression, collapse may be fatal. 

Grishin, E. Polypeptide neurotoxins from spider venoms. Eur. J. Biochem. 1999, 264,... 

An expert extracts venom from a snake, which will later be used to create antivenom for snake bite victims. Snakes can have different types of venom neurotoxins or cytotoxins. Neurotoxins work by blocking nerve function, while cytotoxins destroy cells directly. 

Table 2 Biological activity and detection methods for neurotoxins from venomous animals ...

Neurotoxins from snake venoms have proved to be valuable tools for the understanding of synaptic transmission mechanisms. Likewise, the powerful inhibitory action of fasciculins against mammalian AChE makes them potentially useful for pharmacological and neurochemical research. Studies of their biochemical and electrophysiological effects on the CNS and biochemical characterization are now being carried out. 

Aird, S. D., Middaugh, C. R., and Kaiser, I. I. (1989b). Spectroscopic characterization of textilotoxin, a presynaptic neurotoxin from the venom of the Australian eastern brown snake (Pseudonaja t. textilis). Biochim. Biophys. Acta 997 219-223. 

Faure, G., Guillaume, J. L., Camoin, L., Saliou, B., and Bon, C. (1991). Multiplicity of acidic subunit isoforms of crotoxin, the phospholipase A2 neurotoxin from Crotalus durissus terrificus venom, results from post translational modifications. Biochemistry 30 8074-8083. 

Liu, C.-S., Chen, J.-R, Chang, C.-S., and Lo, T.-B. (1989b). Amino acid sequence of a short chain neurotoxin from the venom of banded krait. J. Biochem. 105 93-97. 

Mori, N., and Tu, A. T. (1988b). Amino acid sequence of the minor neurotoxin from Acalytophis peronii venom. Biol. Chem. Hoppe-Seyler 369 521-526. 

Tu, A. T. (1990). Neurotoxins from sea snake and other vertebrate venoms. In Marine Toxins Origin, Structure, and Molecular Pharmacology (S. Hall and G. Strinchartz, eds.). ACS Symp. Ser. 418 336-346. 

In our laboratory we first isolated the major lethal protein (termed Cobrotoxin) of non-enzymatic nature from the venom of Taiwan cobra Naja naja atra) in 1964 and subsequently purified and crystallized the protein. The primary structure and the disulfide linkages with various efforts by chemical modification and immunological methods in elucidation of the structure-function relationship of this important venom neurotoxin have since been accomplished. Structure-activity correlations have been drawn from chemical modification carried out on both pre- and post-synaptic neurotoxins. With recent advances in DNA recombination and protein engineering, we feel that the time is now ripe to apply these techniques to the isolation and characterization of the genes encoding these toxins. Detailed structural and site-specific mutational studies on the cDNA clones of neurotoxins of both types may complement our previous chemical modifications of the functional role of some amino acid residues in neurotoxins and lead to insight into the modes of action for these biologically active molecules. 

Ducancel, F., Guignery-Frelat, G., Boulain, J.C. and Menez, A. (1990) Nucleotide sequence and structure analysis of cDNA encoding short-chain neurotoxins from venom glands of sea snake (Aipysurus laevis). Toxicon 2S 119-123. 

Endo, T. and Tamiya, N. (1991) Structure-function relationships of postsynaptic neurotoxins from snake venoms, in Snake Toxins " (Harvey, A.L., ed.) Pergamon Press, New York, pp. 165-222. 

Endo T., Oya, M., Tamiya, N. and Hayashi, K. (1987) Role of C-terminal tail of long neurotoxins from snake venoms in molecular conformation and acetylcholine receptor binding Protein nuclear magnetic resonance and competition binding studies. Biochemistry 26 4592-4598. 

Walkinshaw, M. D., Saenger, W. and Maelicke, A. (1980) Three-dimensional structure of the long neurotoxin from cobra venom. Proc. Natl. Acad. Sci. USA 11 2400-2404. 

EVOLUTIONARY RELATIONSHIPS OF p-NEUROTOXINS CROTOXIN CA CAN INTERFERE WITH SINGLE CHAIN p-NEUROTOXINS FROM VIPERIDAE VENOMS AND MODIFY THEIR PHYSIOLOGICAL PROPERTIES... 

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