Rabies lyssavirus glycoprotein (RABV-G)

The Rabies lyssavirus glycoprotein is the sole protein expressed on the surface of the rabies virus, forming characteristic homotrimeric spikes that are essential for viral infectivity. It mediates the initial attachment of the virus to host cell receptors, including the nicotinic acetylcholine receptor (nAChR), neural cell adhesion molecule (NCAM), and p75 neurotrophin receptor (p75NTR), which facilitates the virus's profound neurotropism. Upon endocytosis, the protein undergoes a pH-dependent conformational change from a pre-fusion to a post-fusion state, triggering the fusion of the viral envelope with the endosomal membrane to release the viral genome into the cytoplasm. As the primary target for neutralizing antibodies, this glycoprotein is the central component of all modern rabies vaccines and the target for passive immunotherapy using rabies immune globulins and monoclonal antibodies. Therapeutic strategies focus on blocking these surface proteins to prevent viral entry and spread within the central nervous system.

Other names

Glycoprotein GRabies G proteinRABV-GSpike glycoprotein GRabies virus glycoprotein

Neutralization of viral particles, inhibition of receptor binding, and prevention of pH-dependent endosomal membrane fusion.