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GP  -  virion spike glycoprotein precursor

Zaire ebolavirus

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Disease relevance of GP

  • When GP expressed from vaccinia virus vectors was analyzed by pulse-chase experiments, the mature form and two different precursors were identified [1].
  • Vector-expressed GP formed spikes morphologically indistinguishable from spikes on virus particles, indicating that spike assembly is independent of other viral proteins [2].
  • GP was expressed by means of recombinant baculoviruses in Spodoptera frugiperda cells [3].
  • To determine the functional significance of the coiled-coil motif of GP2, we examined the effects of peptides corresponding to the coiled-coil motif of GP2 on the infectivity of a mutant vesicular stomatitis virus (lacking the receptor-binding/fusion protein) pseudotyped with the Ebola virus GP [4].
  • Pseudotype viruses prepared with a luciferase-containing human immunodeficiency virus type 1 backbone and packaged by the MBG virus or the Zaire subtype EBO virus glycoproteins (GP) mediated infection of a comparable wide range of mammalian cell types, and both were inhibited by ammonium chloride [5].

High impact information on GP


Chemical compound and disease context of GP

  • Maturation and release of the Ebola virus glycoprotein GP were studied in cells infected with either Ebola or recombinant vaccinia viruses [2].
  • Entry and fusion of Ebola virus GP pseudotypes, but not VSV-G or HIV-1 Env pseudotypes, were impaired in the presence of the microtubule-disrupting agent nocodazole but were enhanced in the presence of the microtubule-stabilizing agent paclitaxel (Taxol) [8].
  • In lectin binding studies, the insect cell culture-derived GPs were found to differ from mammalian cell derived virion GP, in that they had no complex/hybrid N-linked glycans or glycans containing sialic acid [9].

Biological context of GP

  • Irrespective of the number of uridine residues at the editing site, all plaque-purified clones of EBOV variant 8mc resembled each other in their pathogenicity for guinea pigs, indicating either the absence or only supportive role of mutations in the GP gene on the adaptation process [10].
  • Studies employing site-directed mutagenesis revealed that GP was cleaved at a multibasic amino acid motif located at positions 497 to 501 of the ORF [1].
  • GP selectively decreased the expression of cell surface molecules that are essential for cell adhesion and immune function [11].
  • GP also decreased cell surface expression of major histocompatibility complex class I molecules, which alters recognition by immune cells, and this effect was also dependent on the mucin domain previously implicated in GP cytotoxicity [11].
  • When the Ebola virus glycoprotein (GP) responsible for receptor binding and membrane fusion was expressed in cells, we found pleomorphic particles budding from the plasma membrane [12].

Anatomical context of GP

  • Expression of EV GP by these recombinant viruses resulted in its efficient incorporation into virus particles and increased cytopathic effect in Vero cells [13].
  • GP derived from the Reston strain of virus, which causes disease in nonhuman primates but not in man, did not disrupt the vasculature of human blood vessels [6].
  • Ebola virions contain a surface transmembrane glycoprotein (GP) that is responsible for binding to target cells and subsequent fusion of the viral and host-cell membranes [14].
  • We identified cell lines and primary cell types such as macrophages that were readily infected by GP pseudotypes despite lacking detectable surface FRalpha, indicating that this receptor is not essential for Ebola virus infection [15].
  • This unexpected feature, possibly related to the nature of the EboV receptor, could explain the impossibility of inducing formation of syncytia among GP-expressing cells [16].

Associations of GP with chemical compounds

  • Three of five viral clones showed insertion of one uridine residue at the GP gene-editing site, which led to a significant change in the expression of virus glycoproteins [10].
  • In the present study, we have investigated processing and maturation of the envelope glycoprotein (GP) of Ebola virus [1].
  • Likewise, removal of two acylated cysteine residues in the transmembrane region of GP showed no discernible effects on infectivity [17].
  • We next introduced alanine substitutions into hydrophobic residues in the coiled-coil motif to identify residues important for GP function [4].
  • Modulation of N-glycans on Env or GP through production of viruses in different primary cells or in the presence of the mannosidase I inhibitor deoxymannojirimycin dramatically affected DC-SIGN(R) infectivity enhancement [18].

Other interactions of GP

  • GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases [19].
  • Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP [12].
  • The Ebola nucleoprotein (NP) or glycoprotein (GP) genes were introduced into the VEE RNA downstream from the VEE 26S promoter in place of the VEE structural protein genes [20].

Analytical, diagnostic and therapeutic context of GP

  • Ebola virus-like particles (VLPs) were produced by coinfection of Sf9 cells with rBV-VP40 and rBV-GP, and incorporation of Ebola GP into VLPs was demonstrated by SDS-PAGE and Western blot analysis [21].
  • To determine whether this earlier immune response could nonetheless protect against disease, cynomolgus macaques were challenged with Ebola virus after vaccination with ADV-GP and nucleoprotein (NP) vectors [22].
  • Fusion was not observed when target cells underwent acidic treatment, for example, when they were placed in coculture with GP-expressing cells before the activation step [16].
  • To provide the virions with enhanced tropism for the lung, LVs were pseudotyped with the Zaire strain of the Ebola virus glycoprotein (EboZ GP) and delivered by endotracheal intubation [23].
  • Partial protection could be observed for at least 9 months after three immunizations with 0.5 microgram of the GP DNA vaccine [24].


  1. Processing of the Ebola virus glycoprotein by the proprotein convertase furin. Volchkov, V.E., Feldmann, H., Volchkova, V.A., Klenk, H.D. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  2. Release of viral glycoproteins during Ebola virus infection. Volchkov, V.E., Volchkova, V.A., Slenczka, W., Klenk, H.D., Feldmann, H. Virology (1998) [Pubmed]
  3. Recombinant Ebola virus nucleoprotein and glycoprotein (Gabon 94 strain) provide new tools for the detection of human infections. Prehaud, C., Hellebrand, E., Coudrier, D., Volchkov, V.E., Volchkova, V.A., Feldmann, H., Le Guenno, B., Bouloy, M. J. Gen. Virol. (1998) [Pubmed]
  4. Functional importance of the coiled-coil of the Ebola virus glycoprotein. Watanabe, S., Takada, A., Watanabe, T., Ito, H., Kida, H., Kawaoka, Y. J. Virol. (2000) [Pubmed]
  5. Distinct mechanisms of entry by envelope glycoproteins of Marburg and Ebola (Zaire) viruses. Chan, S.Y., Speck, R.F., Ma, M.C., Goldsmith, M.A. J. Virol. (2000) [Pubmed]
  6. Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury. Yang, Z.Y., Duckers, H.J., Sullivan, N.J., Sanchez, A., Nabel, E.G., Nabel, G.J. Nat. Med. (2000) [Pubmed]
  7. Recovery of infectious Ebola virus from complementary DNA: RNA editing of the GP gene and viral cytotoxicity. Volchkov, V.E., Volchkova, V.A., Muhlberger, E., Kolesnikova, L.V., Weik, M., Dolnik, O., Klenk, H.D. Science (2001) [Pubmed]
  8. Studies of ebola virus glycoprotein-mediated entry and fusion by using pseudotyped human immunodeficiency virus type 1 virions: involvement of cytoskeletal proteins and enhancement by tumor necrosis factor alpha. Yonezawa, A., Cavrois, M., Greene, W.C. J. Virol. (2005) [Pubmed]
  9. Comparison of the protective efficacy of DNA and baculovirus-derived protein vaccines for EBOLA virus in guinea pigs. Mellquist-Riemenschneider, J.L., Garrison, A.R., Geisbert, J.B., Saikh, K.U., Heidebrink, K.D., Jahrling, P.B., Ulrich, R.G., Schmaljohn, C.S. Virus Res. (2003) [Pubmed]
  10. Molecular characterization of guinea pig-adapted variants of Ebola virus. Volchkov, V.E., Chepurnov, A.A., Volchkova, V.A., Ternovoj, V.A., Klenk, H.D. Virology (2000) [Pubmed]
  11. Ebola virus glycoprotein toxicity is mediated by a dynamin-dependent protein-trafficking pathway. Sullivan, N.J., Peterson, M., Yang, Z.Y., Kong, W.P., Duckers, H., Nabel, E., Nabel, G.J. J. Virol. (2005) [Pubmed]
  12. Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP. Noda, T., Sagara, H., Suzuki, E., Takada, A., Kida, H., Kawaoka, Y. J. Virol. (2002) [Pubmed]
  13. A single intranasal inoculation with a paramyxovirus-vectored vaccine protects guinea pigs against a lethal-dose Ebola virus challenge. Bukreyev, A., Yang, L., Zaki, S.R., Shieh, W.J., Rollin, P.E., Murphy, B.R., Collins, P.L., Sanchez, A. J. Virol. (2006) [Pubmed]
  14. Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution. Malashkevich, V.N., Schneider, B.J., McNally, M.L., Milhollen, M.A., Pang, J.X., Kim, P.S. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  15. Folate receptor alpha and caveolae are not required for Ebola virus glycoprotein-mediated viral infection. Simmons, G., Rennekamp, A.J., Chai, N., Vandenberghe, L.H., Riley, J.L., Bates, P. J. Virol. (2003) [Pubmed]
  16. Detection of cell-cell fusion mediated by Ebola virus glycoproteins. Bär, S., Takada, A., Kawaoka, Y., Alizon, M. J. Virol. (2006) [Pubmed]
  17. Ebola virus glycoprotein: proteolytic processing, acylation, cell tropism, and detection of neutralizing antibodies. Ito, H., Watanabe, S., Takada, A., Kawaoka, Y. J. Virol. (2001) [Pubmed]
  18. Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR. Lin, G., Simmons, G., Pöhlmann, S., Baribaud, F., Ni, H., Leslie, G.J., Haggarty, B.S., Bates, P., Weissman, D., Hoxie, J.A., Doms, R.W. J. Virol. (2003) [Pubmed]
  19. GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases. Volchkov, V.E., Becker, S., Volchkova, V.A., Ternovoj, V.A., Kotov, A.N., Netesov, S.V., Klenk, H.D. Virology (1995) [Pubmed]
  20. Recombinant RNA replicons derived from attenuated Venezuelan equine encephalitis virus protect guinea pigs and mice from Ebola hemorrhagic fever virus. Pushko, P., Bray, M., Ludwig, G.V., Parker, M., Schmaljohn, A., Sanchez, A., Jahrling, P.B., Smith, J.F. Vaccine (2000) [Pubmed]
  21. Ebola virus-like particles produced in insect cells exhibit dendritic cell stimulating activity and induce neutralizing antibodies. Ye, L., Lin, J., Sun, Y., Bennouna, S., Lo, M., Wu, Q., Bu, Z., Pulendran, B., Compans, R.W., Yang, C. Virology (2006) [Pubmed]
  22. Accelerated vaccination for Ebola virus haemorrhagic fever in non-human primates. Sullivan, N.J., Geisbert, T.W., Geisbert, J.B., Xu, L., Yang, Z.Y., Roederer, M., Koup, R.A., Jahrling, P.B., Nabel, G.J. Nature (2003) [Pubmed]
  23. Functional expression of mouse relaxin and mouse relaxin-3 in the lung from an Ebola virus glycoprotein-pseudotyped lentivirus via tracheal delivery. Silvertown, J.D., Walia, J.S., Summerlee, A.J., Medin, J.A. Endocrinology (2006) [Pubmed]
  24. DNA vaccines expressing either the GP or NP genes of Ebola virus protect mice from lethal challenge. Vanderzanden, L., Bray, M., Fuller, D., Roberts, T., Custer, D., Spik, K., Jahrling, P., Huggins, J., Schmaljohn, A., Schmaljohn, C. Virology (1998) [Pubmed]
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