Ebola virus Glycoprotein Proteins, Antibodies, cDNA Clones Research Reagents

All Ebola virus Glycoprotein reagents are produced in house and quality controlled, including 18 Ebola virus Glycoprotein Antibody, 62 Ebola virus Glycoprotein Gene, 9 Ebola virus Glycoprotein IP Kit, 24 Ebola virus Glycoprotein Lysate, 24 Ebola virus Glycoprotein Protein. All Ebola virus Glycoprotein reagents are ready to use.

Ebola virus Glycoprotein Protein (24)

    Ebola virus Glycoprotein Antibody (18)

      Ebola virus Glycoprotein cDNA Clone (62)

      Subtype Zaire, strain Mayinga 1976
      subtype Reston, strain Pennsylvania or Reston
      subtype Tai Forest, strain Cote d'Ivoire-94
      Subtype Bundibugyo, strain Uganda 2007
      Subtype Sudan, strain Gulu

      In expression vector

      In lentiviral vector

      subtype Zaire, strain H.sapiens-wt/GIN/2014/K

      In expression vector

      In lentiviral vector

      Ebola virus Glycoprotein Lysate (24)

        Ebola virus Glycoprotein Background

        The fourth gene of the EBOV genome encodes a 16-kDa envelope-attached glycoprotein (GP) and a 11 kDa secreted glycoprotein (sGP). Both GP and sGP have an identical 295-residue N-terminus, however, they have different C-terminal sequences. Recently, great attention has been paid to GP for vaccines design and entry inhibitors isolation. GP is a class I fusion protein which assembles as trimers on viral surface and plays an important role in virus entry and attachment. Mature GP is a disulfide-linked heterodimer formed by two subunits, GP1 and GP2, which are generated from the proteolytical process of GP precursor (pre-GP) by cellular furin during virus assembly . The GP1 subunit contains a mucin domain and a receptor-binding domain (RBD); the GP2 subunit has a fusion peptide, a helical heptad-repeat (HR) region, a transmembrane (TM) domain, and a 4-residue cytoplasmic tail. The RBD of GP1 mediates the interaction of EBOV with cellular receptor (e.g. DC-SIGN/LSIGN, TIM-1, hMGL, NPC1, β-integrins, folate receptor-α, and Tyro3 family receptors), of which TIM1 and NPC1 are essential for EBOV entry; the mucin domain having N- and O-linked glycans enhances the viral attachment to cellular hMGL, and participates in shielding key neutralization epitopes, which helps the virus evades immune elimination. There are large conformation changes of GP2 during membrane fusion, which enhance the insertion of fusion loop into cellular membrane and facilitate the release of viral nucleocapsid core to cytoplasm.

        Ebola virus Glycoprotein References

        • Volchkov VE, et al. Processing of the Ebola virus glycoprotein by the proprotein convertase furin. Proc Natl Acad Sci U S A. 1998 May 12;95(10):5762-7.
        • Lee JE, et al. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature. 2008 Jul 10;454(7201):177-82. doi: 10.1038/nature07082.
        • Hood CL, et al. Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity. J Virol. 2010 Mar;84(6):2972-82. doi: 10.1128/JVI.02151-09.
        • Cook JD and Lee JE. The secret life of viral entry glycoproteins: moonlighting in immune evasion. PLoS Pathog. 2013 May;9(5):e1003258. doi: 10.1371/journal.ppat.1003258.
        • Miller EH and Chandran K. Filovirus entry into cells - new insights. Curr Opin Virol. 2012 Apr;2(2):206-14. doi: 10.1016/j.coviro.2012.02.015.

        Note: Flag® is a registered trademark of Sigma Aldrich Biotechnology LP. It is used here for informational purposes only.