EBOLA VIRUS ENVELOPE GLYCOPROTEIN (GP1) MUCIN-LIKE REGION (ZAIRE)
Ebola Virus Envelope Glycoprotein GP1 Mucin-Like Region (Zaire) is a recombinant protein expressed and purified from E. coli.
PRODUCT DETAILS – EBOLA VIRUS GP1 MUCIN-LIKE REGION (ZAIRE)
- Recombinant protein containing 181 amino acids of the mucin-like region (Emuc) from EBOV (Zaire, strain Kikwit-95).
- Protein produced in E. coli and fused to a 6xHis-tag at its C-terminus, with a molecular weight of 38kDa. Protein is purified by a proprietary chromatographic technique.
- Greater than 95% purity as determined by SDS-PAGE (Coomassie-stained).
- Presented in phosphate buffer with 25mM arginine and 0.02% sodium azide.
Ebolavirus (EBOV) and Marburg virus cause fatal hemorrhagic fevers in humans, with high mortality rates. Therefore, much effort has been focused on developing vaccines and therapeutics to prevent and treat filoviral infections.
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.
- 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.