Anti-Bundibugyo Ebolavirus, GP (Clone BDBV-317) - Purified No Carrier Protein (E169-GRP)

Ebola virus is a member of the Filoviridae family that causes severe disease in humans with a mortality rate of 25-90%1. Three Ebola species are responsible for lethal outbreaks: Zaire ebolavirus (EBOV), Bundibugyo ebolavirus (BDBV), and Sudan ebolavirus (SUDV). The Ebola virus envelope contains a single surface glycoprotein (GP) which is responsible for viral attachment to the host cell, endosomal entry, and membrane fusion1. GP is composed of two subunits, GP1 and GP2. GP1 has a heavily glycosylated mucin-like domain and a glycan cap. GP2 contains the internal fusion loop, transmembrane domain, and stalk. GP is the major target of neutralizing monoclonal antibody (mAb) and vaccine design against Ebola virus1,2,3. BDBV-317 is a GP mAb isolated from B cells of a survivor of the 2007 Uganda BDBV outbreak3. Peripheral blood mononuclear cells from the survivor were transformed with Epstein-Barr virus, CpG, and additional supplements. Subsequently, cell supernatants were screened by ELISA for binding to GPs from BDBV, EBOV, or MARV filoviruses. Positive cells were fused with HMMA2.5 myeloma cells by electrofusion and cloned by single-cell fluorescence-activated cell sorting. BDBV-317 binds to and neutralizes BDBV as well as EBOV heterologous Mayinga (historical) and Makona-Gueckedou-C07 (contemporary) strains3,4. BDBV-317 also neutralizes two strains of Reston virus and recognizes, but does not neutralize, SUDV4. BDBV-317 can also recognize a linear synthesized peptide spanning GP amino acids 620-635, suggesting a relatively linear epitope in vivo4. A single critical contact residue in GP2 (K633) is located in a region that spans the C-terminal part of HR2 and the N-terminal part of MPER4. Three BDBV-317 molecules bind simultaneously to the GP trimer4. BDBV-317 provides complete protection from death against EBOV (Mayinga strain) in mouse and partial protection in guinea pig4.