Ebola Virus Envelope Glycoprotein GP1 Subunit (subtype Bundibugyo, strain Uganda 2007) (recombinant)

Ebola virus (EBOV) is an enveloped and negative-stranded RNA virus, a member of the Ebolavirus genus, and the causative agent of Ebola virus disease (EVD), a condition characterized by a hemorrhagic fever and a high mortality rate, that is endemic to western and equatorial Africa.¹ The single-stranded RNA genome of EBOV encodes seven proteins: nucleoprotein (NP), virion protein 40 (VP40), VP35, VP30, VP24, glycoprotein (GP), and an RNA-dependent RNA polymerase (L).^1,2 EBOV envelope GP is a class I fusion protein involved in viral attachment and entry to host cells.³ It is composed of two subunits, GP1 and GP2, which are separated by a furin cleavage site and linked via disulfide bonds to form trimers of heterodimers with a chalice and cradle-like structure.^4,3,5 EBOV GP is covered with N- and O-linked glycans, and the GP1 subunit is composed of a signal peptide, base, and head domains, a glycan cap, which shields the receptor-binding site, and a mucin-like domain, which is heavily glycosylated with O-linked glycans.^4,3 The GP1 subunit is involved in host cell attachment, and cleavage of the glycan cap and mucin-like domain by host cathepsin B, with cathepsin L in an accessory role, is required for binding to the host cell.^3,6 Once fused, the EBOV virion enters the cell via macropinocytosis and is transported to the endosome. The glycosylation of the glycan cap and dense glycosylation of the GP1 mucin-like domain shield surface epitopes and prevent neutralizing antibodies from interacting with regions required for host cell binding, fusion, and entry.^7,5 Cayman's Ebola Virus Envelope Glycoprotein GP1 Subunit (subtype Bundibugyo, strain Uganda 2007) (recombinant) protein consists of 480 amino acids, has a calculated molecular weight of 53.5 kDa, and a predicted N-terminus of Ile33 after signal peptide cleavage. By SDS-PAGE, under reducing conditions (if applicable), the apparent molecular mass of the protein is approximately 75 kDa due to glycosylation.

WARNING This product is not for human or veterinary use.

1. Rojas, M., Monsalve, D.M., Pacheco, Y., et al. Ebola virus disease: An emerging and re-emerging viral threat. J. Autoimmun. 106, 102375 (2020).

2. Salata, C., Calistri, A., Alvisi, G., et al. Ebola virus entry: From molecular characterization to drug discovery. Viruses 11(3), 274 (2019).

3. Hood, C.L., Abraham, J., Boyington, J.C., et al. Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: Implications for viral entry and immunogenicity. J. Virol. 84(6), 2972-2982 (2010).

4. Lee, J.E., Fusco, M.L., Hessell, A.J., et al. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 454(7201), 177-182 (2008).

5. Cook, J.D., and Lee, J.E. The secret life of viral entry glycoproteins: Moonlighting in immune evasion. PLoS Pathog. 9(5), e1003258 (2013).

6. Miller, E.H., and Chandran, K. Filovirus entry into cells - New insights. Curr. Opin. Virol. 2(2), 206-214 (2012).

7. Iraqi, M., Edri, A., Greenshpan, Y., et al. N-glycans mediate the Ebola virus-GP1 shielding of ligands to immune receptors and immune evasion. Front. Cell. Infect. Microbiol. 10, 48 (2020).