Rabies virus binding to the nicotinic acetylcholine receptor alpha subunit demonstrated by virus overlay protein binding assay.
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 alpha-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 alpha-bungarotoxin. In blots of affinity-purified AChR, labelled virus bound to the 40 kDa alpha subunit and was competed by alpha-bungarotoxin. Based on binding of rabies virus to the alpha subunit and the ability of alpha-bungarotoxin to compete for binding, rabies virus appears to bind to the neurotoxin-binding site of the nicotinic AChR alpha subunit.
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520-8002, USA.
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M
Gastka
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Horvath
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TL
Lentz
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002038:Bungarotoxins / Q000378:metabolism; D004557:Electric Organ / Q000378:metabolism*; D011820:Rabies virus / Q000378:metabolism*; D011978:Receptors, Nicotinic / Q000378:metabolism*; D011991:Receptors, Virus / Q000378:metabolism*; D014101:Torpedo / Q000378:metabolism*
D002038:Bungarotoxins; D011978:Receptors, Nicotinic; D011991:Receptors, Virus