Anti-Rabies virus Antibody, clone 802 clone 802, from mouse

Glycoprotein (UniProt: P03524) of Rabies virus of Evelyn-Rokitnicki-Abelseth (ERA) strain is encoded by the G gene. Rabies virus belongs to the Lyssavirus serogroup of viruses. The glycoprotein of Rabies virus is a homotrimer, single-pass type I membrane protein that attaches the virus to host cellular receptor and thereby inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane. It has been shown that the nicotinic acetylcholine receptor (nAChR), the neuronal cell adhesion molecule (NCAM), and the p75 neurotrophin receptor (p75NTR) bind glycoprotein and facilitate Rabies virus entry into cells. Arginine 352 is considered to be highly involved in Rabies virus pathogenicity and a mutation at this site dramatically attenuates the virus. Rabies virus glycoprotein is synthesized with a signal peptide (aa 1-19) that is subsequently cleaved off. It has two topological domains (aa 20-459 virion surface; 481-524 intravirion) and a helical domain (aa 460-480). Glycosylation of viral glycoprotein is considered to be crucial for glycoprotein export at the cell surface. Clone 802 is shown to recognize most Rabies virus strains, however it does not display neutralizing activity. (Ref.: Schumacher, CL et al. (1989). J. Clin. Invest. 84(3); 971-975; Bunschoten, H et al. (1989). J. Gen. Virol. 70(2); 291-298).