Amino acid sequence similarity between rabies virus glycoprotein and snake venom curaremimetic neurotoxins.
Evidence was presented earlier that a host-cell receptor for the highly neurotropic rabies virus might be the acetylcholine receptor. The amino acid sequence of the glycoprotein of rabies virus was compared by computer analysis with that of snake venom curaremimetic neurotoxins, potent ligands of the acetylcholine receptor. A statistically significant sequence relation was found between a segment of the rabies glycoprotein and the entire sequence of long neurotoxins. The greatest identity occurs with residues considered most important in neurotoxicity, including those interacting with the acetylcholine binding site of the acetylcholine receptor. Because of the similarity between the glycoprotein and the receptor-binding region of the neurotoxins, this region of the viral glycoprotein may function as a recognition site for the acetylcholine receptor. Direct binding of the rabies virus glycoprotein to the acetylcholine receptor could contribute to the neurotropism of this virus.
D000595:Amino Acid Sequence; D000818:Animals; D006023:Glycoproteins / Q000235:genetics*; D009498:Neurotoxins / Q000235:genetics*; D011820:Rabies virus / Q000235:genetics*; D011950:Receptors, Cholinergic / Q000378:metabolism; D012910:Snake Venoms / Q000235:genetics*; D012911:Snakes; D014764:Viral Proteins / Q000235:genetics*
D006023:Glycoproteins; D009498:Neurotoxins; D011950:Receptors, Cholinergic; D012910:Snake Venoms; D014764:Viral Proteins