Rabies Virus Glycoprotein

The membrane of rabies virus is composed of a lipid bilayer and one glycoprotein. The glycoprotein of Rabies Virus is found to be located on the external surface of the viral membrane. It is comprised of four domains: signal peptide (SP), ectodomain (ED), transmembrane (TM), and a cytoplasmic domain (CD). The G-protein is 65 kDa and contains 524 amino acids. Due to the presence of its signal peptide (SP), it is located on the N-terminal and spans 19 residues. The SP is responsible for anchoring the protein to the ER-Golgi Apparatus (AP) membrane. This promotes subsequent transport of the nascent protein to the membrane before it is cleaved from the N-terminus in the AP.
The rabies virus glycoprotein contains three oligosaccharide side chains that account for about 11% of its total mass. This glycoprotein preparation not only reacts with and induces the production of rabies neutralizing antibodies but also protects mice in vaccination experiments from a challenge infection with rabies virus. The glycoprotein vaccine had similar or better protective activity than a vaccine made from inactivated virus
The rabies virus glycoprotein in each peak is anchored in the plasma membrane and the lipid envelope by the transmembrane domain of 22 amino acids from 439 to 461 residues. The C-terminal with the final 44 amino acids is the cytoplasmic domain. It extends into the cytoplasm of the infected cell where it interacts with the methionine to complete the viral assembly.