Polypeptide neurotoxins

Turning now to chemical attack, many predators immobilize their prey by injecting toxins, often neurotoxins, into them. Examples include venomous snakes, spiders, and scorpions. Some spider toxins (Quick and Usherwood 1990 Figure 1.3) are neurotoxic through antagonistic action upon glutamate receptors. The venom of some scorpions contains polypeptide neurotoxins that bind to the sodium channel. 

Actinia cari toxins, 308 Actiniaria, carotenoids, 320 Actinodendron plumosuniy polypeptide neurotoxins, 194 Actinopyga aglycones, 320 holothurins, 320 Activators... 

Renaud J-F, Fosset M, Schweitz H, Lazdunski M. The interaction of polypeptide neurotoxins with tetrodotoxin-resistant Na+ channels in mammalian cardiac cells. 

Howard BD, Gundersen CBJ (1980) Effects and mechanisms of polypeptide neurotoxins that act presynaptically. Annu Rev Pharmacol Toxicol 20 307-36 Huang X, Wheeler MB, Kang YH, Sheu L, Lukacs GL et al. (1998) Truncated SNAP-25 (1-197), like botulinum neurotoxin A, can inhibit insulin secretion from HIT-T15 insulinoma cells. Mol Endocrinol 12 1060-70... 

Polypeptide neurotoxin from the Australian tiger snake (Notechis scutatus scutatus). Prevents release of ACh from nerve endings paralyses muscles. 

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

Kem, W.R. 1976. Purification and characterization of a new family of polypeptide neurotoxins from the heteronemertine Cerebratulus lacteue Leidy. J. Biol. Chem. 251, 4184-4192. 

THE COMPOSITE PHYSICAL AND CHEMICAL APPROACH TO THE SOLUTION SPATIAL STRUCTURE OF POLYPEPTIDE NEUROTOXINS... 

This paper presents the results of the composite physical and chemical approach, with the main stress on NMR spectroscopy data, in an analysis of the spatial structure of some polypeptide neurotoxin components of bee and snake venoms - apamin and short neurotoxins, respectively. 

Catterall, W. a., and D. A. Beneski Interaction of polypeptide neurotoxins with a receptor site associated with voltage-sensitive sodium channels. J. Supramol. Struct. 14, 295—304 (1980). 

Lawrence, J. C., and W. A. Catterall Textrodotoxin-insensitive sodium channels. Binding of polypeptide neurotoxins in primary cultures of rat muscle cells. J. Biol. Chem. 256, 6223—6229 (1981). 

Botulism, the deadly food poisoning disease is caused by the growth of various strains of Clostridium botulinum in food. The organism produces a large polypeptide (neurotoxin) which is the most toxic protein known to the human kind. Seven serotypes of botulinum neurotoxins produced by different strains of C. botulinum have been characterized, and serotypes A, B and E are known to cause botulism in humans. Ingestion of food contaminated with the neurotoxin causes flaccid muscle paralysis that can result in patients death. Wound botulism has also been reported where the organism can grow in the wounds, and produces the neurotoxin that causes paralysis. 

Monks, S.A., Gould, A.R., Lumley, P.E., Alewood, P.F., Kern, W.R., Goss, N.H., and Norton, R.S., 1994, Limited Proteolysis Study of Structure-function Relationships in Shi, a Polypeptide Neurotoxin from a Sea Anemone, In Biochim.Biophys.Acta, 1207, 93-101. 

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