Binding of rabies virus to purified Torpedo acetylcholine receptor.
The binding of 125I- and 35S-labeled rabies virus (CVS strain) to affinity-purified acetylcholine receptor from Torpedo electric organ was demonstrated. The binding of rabies virus to the acetylcholine receptor increased with increasing receptor concentration, was dependent on the pH of the incubation medium, and was saturable with increasing virus concentration. Binding of radioactively labeled virus was effectively competed by unlabeled homologous virus particles. Binding of 35S-labeled rabies virus to the AChR was inhibited up to 50% by alpha-bungarotoxin and up to 30% by (+)-tubocurarine but was not affected by atropine. These results demonstrate direct binding of rabies virus to a well-defined neurotransmitter receptor, namely the acetylcholine receptor and indicate that at least a portion of the virus interaction occurs near the acetylcholine binding site on the receptor. These findings support the hypothesis that the acetylcholine receptor may serve as a rabies virus receptor in vivo.
D000818:Animals; D002038:Bungarotoxins / Q000494:pharmacology; D055598:Chemical Phenomena; D002621:Chemistry; D004557:Electric Organ / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011820:Rabies virus / Q000378:metabolism*; D011950:Receptors, Cholinergic / Q000302:isolation & purification / Q000378:metabolism*; D014403:Tubocurarine / Q000494:pharmacology
D002038:Bungarotoxins; D011950:Receptors, Cholinergic; D014403:Tubocurarine