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Rabies virus binding to the nicotinic acetylcholine receptor subunit demonstrated by virus overlay protein binding assay

Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, PO Box 208002, New Haven, Connecticut 06520-8002, USA

A virus overlay protein binding assay was used to study binding of ¹²⁵I-labelled rabies virus to the acetylcholine receptor (AChR) from Torpedo californica electric organ membranes. After gel electrophoresis of electric organ membranes and transfer of proteins to nitrocellulose, ¹²⁵I-labelled -bungarotoxin, a curaremimetic neurotoxin, bound to a 40 kDa band and ¹²⁵I-labelled rabies virus bound to 51 kDa and 40 kDa bands. Binding of rabies virus to the 40 kDa band was inhibited by unlabelled -bungarotoxin. In blots of affinity-purified AChR, labelled virus bound to the 40 kDa subunit and was competed by -bungarotoxin. Based on binding of rabies virus to the subunit and the ability of -bungarotoxin to compete for binding, rabies virus appears to bind to the neurotoxin-binding site of the nicotinic AChR subunit.

Received 18 April 1996; accepted 13 June 1996.

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