EBOLA VIRUS SECRETED GLYCOPROTEIN (SGP) (Bundibugyo)
Ebola virus secreted glycoprotein protein (sGP) is Ile 33 – Arg 324 (Accession # B8XCN1), fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 34.3 kDa. The protein is expressed in HEK293 cells. DTT-reduced Protein migrates as 40-55 kDa in SDS-PAGE.
PRODUCT DETAILS – EBOLA VIRUS SECRETED GLYCOPROTEIN (SGP) (Bundibugyo)
- Recombinant Ebola virus secreted Glycoprotein (sGP) (NCBI Accession Number: B8XCN1).
- Expressed in HEK293 cells, lyophilised and presented in PBS pH7.4 buffer.
- Greater than 90% pure by SDS-PAGE.
The virulence of EBOV may be partially attributed to the Ebola virus secreted glycoprotein (sGP), which is the main product transcribed from its GP gene. Ebola virus secreted glycoprotein is secreted from infected cells and can be readily detected in the serum of EBOV-infected hosts. Mature sGP is produced from a precursor by proteolytic cleavage by host cell proteases such as furin. sGP monomers bind to each other to form a homodimer. The role of Ebola virus secreted glycoprotein in EBOV pathogenesis is unclear, but is examined in detail by de la Vega et al (2015).
EBOV envelope glycoproteins (GPs) are known to function as one of the crucial factors that determine the differential virulence across the five different EBOV species (Zaire ebolavirus, Sudan ebolavirus, Bundibugyo ebolavirus, Tai Forest ebolavirus, and Reston ebolavirus). GPs are type I transmembrane glycoproteins composed of GP1 and GP2 and all filoviruses display multiple copies of this single membrane-anchored glycoprotein (GP) projecting from their envelopes. GP is a trimer in which each monomer is a disulfide-bonded complex of a receptor binding subunit (GP1) and a fusion subunit (GP2). The Ebola virus GP has been the target of multiple neutralizing antibodies (Ab), several of which are effective in preventing the onset of disease in nonhuman primates when administered as part of a monoclonal Ab (MAb) cocktail 1 or 2 days after viral exposure (reviewed in Baseler et al., 2017).
Ebola virus envelope glycoprotein GP1 mucin-like region (Emuc) is a highly glycosylated region located at the apex and the sides of each glycoprotein monomer (Tran et al., 2014); it is dispensable for EBOV infections in vitro and not highly conserved. It can induce morphological change of adherent cells in vitro and causes distinct cell and tissue damage and acute inflammation in mouse muscles in vivo (Ning et al., 2018). It is believed to have various functions including influencing GP structure, enhancing viral attachment to target cell surfaces, protecting conserved regions of GP, such the receptor binding site, from antibody recognition, and masking immune regulatory molecules, such as major histocompatibility complex 1 (MHC1), on infected cell surfaces. Emuc may also have a cytotoxic function and could be involved in binding to human CLEC10A. It was reported to be essential to the infectivity of ZEBOV (Yang et al., 2000). As such, neutralizing antibodies are often directed against Emuc for potential therapeutic use.
****SHIPPING AND STORAGE NOTIFICATION: This recombinant protein has been lyophilised to maximise stability. It is shipped at ambient temperature, and may be stored for up to 1 year at 4C prior to reconstitution. Following reconstitution it should be stored at -80C. Extensive stability tests have shown no negative effects on antigen performance for 7 days of shipping at ambient temperature.
- Baseler et al. (2017). The Pathogenesis of Ebola Virus Disease. Annual Review of Pathology: Mechanisms of Disease, 12(1), 387–418.
- Ning et al. (2018). Ebola virus mucin-like glycoprotein (Emuc) induces remarkable acute inflammation and tissue injury: evidence for Emuc pathogenicity in vivo. Protein Cell, 9: 389.
- Tran et al. (2014). Spatial Localization of the Ebola Virus Glycoprotein Mucin-Like Domain Determined by Cryo-Electron Tomography. J Virol. 88(18):10958-62.
- Yang et al. (2000). Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury. Nat. Med. 6, 886–889.