Characterization of a snake venom neurotoxin which blocks nicotinic transmission in the avian ciliary ganglion

Abstract

Bungarus multicinctus venom was fractionated by ion exchange chromatography and the various fractions were assayed for their ability to block synaptic transmission through the chick ciliary ganglion. α-Bungarotoxin purified from this venom failed to block transmission at 50μg/ml. A second neurotoxin, which we designate Toxin F, blocked transmission at 1–3μg/ml and also blocked ganglionic depolarizations induced by carbachol. Toxin F was clearly distinguishable from α-bungarotoxin on the basis of molecular weight (estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) and isoelectric point. Binding assays revealed that 125I-labeled toxin F bound to two sites in the ciliary ganglion: one site that was shared by α-bungarotoxin and toxin F and another site that was recognized solely by toxin F. Carbachol and d-tubocurarine displaced only that [ 125I]toxin F bound to the shared site and had no effect on [ 125I]toxin F bound to the site recognized by toxin F alone. The results suggest that toxin F blocks synaptic transmission in the chick ciliary ganglion by a postsynaptic mechanism. Further study is required to determine whether this effect of toxin F is mediated through a direct interaction with ganglionic nicotinic receptors.