Abstract The attachment of the spike glycoprotein of rabies virus to a cell surface constituent that is largely restricted to neurons may help explain the neurotropism of this virus. Rabies virus has been localized to regions containing a high density of ACh receptors at neuromuscular junctions and on cultured embryonic myotubes. Recently, a statistically significant amino acid sequence homology was found between a segment of the rabies glycoprotein and the entire sequence of long snake venom curare-mimetic neurotoxins. Because of this similarity, the homologous region of the viral glycoprotein may function as a recognition site for the ACh receptor. While direct binding of the rabies virus glycoprotein to the ACh receptor could contribute to the neurotropism of the virus, the ability of rabies virus to infect a variety of cell types in vitro including many which lack ACh receptors, indicates the virus glycoprotein can attach to other host cell surface components.