Anti-EBOV GP Antibody, clone 1H3 clone 1H3, from mouse

Envelope glycoprotein (UniProt: Q05320; also known as GP1,2; GP) is encoded by the GP gene (Gene ID: 911829) in Zaire Ebola virus. Ebola virus (EBOV) is a filovirus that is shown to cause severe viral hemorrhagic fever with high lethality. It has a single stranded, negative-sense RNA genome that encodes seven viral structural proteins including nucleoprotein, virion proteins, and glycoprotein. The glycoprotein is the most important protein involved in pathogenesis. It is a type I transmembrane surface protein shown to be responsible for receptor binding, viral entry, and cellular tropism. The GP gene is reported to undergo transcriptional editing to give rise to several glycosylated proteins, including the structural protein GP1,2, and the secreted non-structural glycoprotein (sGP). The GP is synthesized as a 676-amino acid polyprotein with a signal peptide (aa 1-32). This polyprotein is cleaved by the furin to yield two disulfide linked subunits known as GP1 (aa 33-501) and GP2 (aa 502-676), which together form the GP1,2 heterodimer. The GP1 acts as the receptor-binding subunit and GP2 as the membrane fusion subunit. The GP1 subunit is expressed on the cell surface with the C-terminus oriented toward the aqueous environment, while the N-terminus is bound to GP2 via disulfide bonds. The GP1 subunit contains the heavily glycosylated mucin-like domain (aa 305-485), which is responsible for its cytotoxic function. The glycoprotein contains two coiled coil regions (aa 554-595 and 615-634) that play a role in its oligomerization and fusion activity. Clone 1H3 recognizes the secreted glycoprotein form (sGP) and also recognizes glycoprotein lacking a large part of the mucin domain (GP1,2 Mucin333 458). It does not recognize VSV G/ZEBOVGP and subfragment D. When administered before virus challenge, it provides only a partial protection. (Ref.: Qiu, X., et al. (2011). Clin. Immunol. 141(2); 218-227).