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Volumn 7, Issue , 2017, Pages

Structure of the Ebola virus glycoprotein spike within the virion envelope at 11 Å resolution

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE GLYCOPROTEIN, EBOLA VIRUS; PROTEIN BINDING; VIRUS ENVELOPE PROTEIN;

EID: 85017404783     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep46374     Document Type: Article
Times cited : (48)

References (41)
  • 2
    • 84908072433 scopus 로고    scopus 로고
    • Ebola virus disease in West Africa-The first 9 months of the epidemic and forward projections
    • Team, W. E. R. Ebola virus disease in West Africa-the first 9 months of the epidemic and forward projections. N. Engl. J. Med. 2014, 1481-1495 (2014).
    • (2014) N. Engl. J. Med. , pp. 1481-1495
    • Team, W.E.R.1
  • 3
    • 84882787658 scopus 로고    scopus 로고
    • Structural rearrangement of ebola virus VP40 begets multiple functions in the virus life cycle
    • Bornholdt, Z. A., et al. Structural rearrangement of ebola virus VP40 begets multiple functions in the virus life cycle. Cell 154, 763-774 (2013).
    • (2013) Cell , vol.154 , pp. 763-774
    • Bornholdt, Z.A.1
  • 4
    • 84855668634 scopus 로고    scopus 로고
    • The organisation of Ebola virus reveals a capacity for extensive, modular polyploidy
    • Beniac, D. R., et al. The organisation of Ebola virus reveals a capacity for extensive, modular polyploidy. PLoS One 7, e29608 (2012).
    • (2012) PLoS One , vol.7 , pp. e29608
    • Beniac, D.R.1
  • 5
    • 84886999873 scopus 로고    scopus 로고
    • How do filovirus filaments bend without breaking
    • Booth, T. F., Rabb, M. J., Beniac, D. R. How do filovirus filaments bend without breaking Trends Microbiol. 21, 583-593 (2013).
    • (2013) Trends Microbiol , vol.21 , pp. 583-593
    • Booth, T.F.1    Rabb, M.J.2    Beniac, D.R.3
  • 6
    • 78149301316 scopus 로고    scopus 로고
    • Cellular entry of ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes
    • Saeed, M. F., Kolokoltsov, A. A., Albrecht, T., Davey, R. A. Cellular entry of ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes. PLoS Pathog 6, e1001110 (2010).
    • (2010) PLoS Pathog , vol.6 , pp. e1001110
    • Saeed, M.F.1    Kolokoltsov, A.A.2    Albrecht, T.3    Davey, R.A.4
  • 7
    • 0031449064 scopus 로고    scopus 로고
    • A system for functional analysis of Ebola virus glycoprotein
    • Takada, A., et al. A system for functional analysis of Ebola virus glycoprotein. Proc. Natl. Acad. Sci. USA. 94, 14764-14769 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 14764-14769
    • Takada, A.1
  • 8
    • 80054774353 scopus 로고    scopus 로고
    • Ebola virus enters host cells by macropinocytosis and clathrin-mediated endocytosis
    • Aleksandrowicz, P., et al. Ebola virus enters host cells by macropinocytosis and clathrin-mediated endocytosis. J. Infect. Dis. 204 Suppl 3, S957-67 (2011).
    • (2011) J. Infect. Dis. , vol.204 , pp. S957-S967
    • Aleksandrowicz, P.1
  • 9
    • 84937022260 scopus 로고    scopus 로고
    • Inhibition of Ebola virus glycoprotein-mediated cytotoxicity by targeting its transmembrane domain and cholesterol
    • Hacke, M., et al. Inhibition of Ebola virus glycoprotein-mediated cytotoxicity by targeting its transmembrane domain and cholesterol. Nature communications 6 (2015).
    • (2015) Nature Communications , vol.6
    • Hacke, M.1
  • 10
    • 80052851832 scopus 로고    scopus 로고
    • Ebola virus entry requires the cholesterol transporter Niemann-Pick C1
    • Carette, J. E., et al. Ebola virus entry requires the cholesterol transporter Niemann-Pick C1. Nature 477, 340-343 (2011).
    • (2011) Nature , vol.477 , pp. 340-343
    • Carette, J.E.1
  • 11
    • 80052868218 scopus 로고    scopus 로고
    • Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection
    • Côté, M., et al. Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection. Nature 477, 344-348 (2011).
    • (2011) Nature , vol.477 , pp. 344-348
    • Côté, M.1
  • 12
    • 78149355646 scopus 로고    scopus 로고
    • Ebolavirus is internalized into host cells via macropinocytosis in a viral glycoprotein-dependent manner
    • Nanbo, A., et al. Ebolavirus is internalized into host cells via macropinocytosis in a viral glycoprotein-dependent manner. PLoS Pathog 6, e1001121 (2010).
    • (2010) PLoS Pathog , vol.6 , pp. e1001121
    • Nanbo, A.1
  • 13
    • 84955572428 scopus 로고    scopus 로고
    • Cross-reactive and potent neutralizing antibody responses in human survivors of natural Ebolavirus infection
    • Flyak, A. I., et al. Cross-reactive and potent neutralizing antibody responses in human survivors of natural Ebolavirus infection. Cell 164, 392-405 (2016).
    • (2016) Cell , vol.164 , pp. 392-405
    • Flyak, A.I.1
  • 14
    • 84978437369 scopus 로고    scopus 로고
    • Toremifene interacts with and destabilizes the Ebola virus glycoprotein
    • Zhao, Y., et al. Toremifene interacts with and destabilizes the Ebola virus glycoprotein. Nature 535, 169-172 (2016).
    • (2016) Nature , vol.535 , pp. 169-172
    • Zhao, Y.1
  • 15
    • 84923350941 scopus 로고    scopus 로고
    • Structural basis for Marburg virus neutralization by a cross-reactive human antibody
    • Hashiguchi, T., et al. Structural basis for Marburg virus neutralization by a cross-reactive human antibody. Cell 160, 904-912 (2015).
    • (2015) Cell , vol.160 , pp. 904-912
    • Hashiguchi, T.1
  • 16
    • 84914127561 scopus 로고    scopus 로고
    • Structures of protective antibodies reveal sites of vulnerability on Ebola virus
    • Murin, C. D., et al. Structures of protective antibodies reveal sites of vulnerability on Ebola virus. Proc. Natl. Acad. Sci. USA. 111, 17182-17187 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA. , vol.111 , pp. 17182-17187
    • Murin, C.D.1
  • 17
    • 77649174605 scopus 로고    scopus 로고
    • Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: Implications for viral entry and immunogenicity
    • Hood, C. L., et al. Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: Implications for viral entry and immunogenicity. J. Virol. 84, 2972-2982 (2010).
    • (2010) J. Virol. , vol.84 , pp. 2972-2982
    • Hood, C.L.1
  • 18
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • Lee, J. E., et al. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 454, 177-182 (2008).
    • (2008) Nature , vol.454 , pp. 177-182
    • Lee, J.E.1
  • 19
    • 84859907529 scopus 로고    scopus 로고
    • Ebola virus entry requires the host-programmed recognition of an intracellular receptor
    • Miller, E. H., et al. Ebola virus entry requires the host-programmed recognition of an intracellular receptor. EMBO J. 31, 1947-1960 (2012).
    • (2012) EMBO J. , vol.31 , pp. 1947-1960
    • Miller, E.H.1
  • 20
    • 33645788357 scopus 로고    scopus 로고
    • Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein
    • Schornberg, K., et al. Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein. J. Virol. 80, 4174-4178 (2006).
    • (2006) J. Virol. , vol.80 , pp. 4174-4178
    • Schornberg, K.1
  • 21
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran, K., Sullivan, N. J., Felbor, U., Whelan, S. P., Cunningham, J. M. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308, 1643-1645 (2005).
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 22
    • 63149192804 scopus 로고    scopus 로고
    • Jh Kuhn u. Jm White (2009): The Primed Ebolavirus Glycoprotein (19-Kilodalton GP1(2): Sequence and residues critical for host cell binding
    • Dube, D., et al. Jh Kuhn u. Jm White (2009): The Primed Ebolavirus Glycoprotein (19-Kilodalton GP1, 2): Sequence and Residues Critical for Host Cell Binding. J. Virol. 83, 2883-2891.
    • J. Virol. , vol.83 , pp. 2883-2891
    • Dube, D.1
  • 23
    • 84928555554 scopus 로고    scopus 로고
    • Role of EXT1 and Glycosaminoglycans in the Early Stage of Filovirus Entry
    • O'Hearn, A., et al. Role of EXT1 and Glycosaminoglycans in the Early Stage of Filovirus Entry. J. Virol. 89, 5441-5449 (2015).
    • (2015) J. Virol. , vol.89 , pp. 5441-5449
    • O'Hearn, A.1
  • 24
    • 0033020204 scopus 로고    scopus 로고
    • Core structure of the envelope glycoprotein GP2 from Ebola virus at 1. 9-A resolution
    • Malashkevich, V. N., et al. Core structure of the envelope glycoprotein GP2 from Ebola virus at 1. 9-A resolution. Proc. Natl. Acad. Sci. USA. 96, 2662-2667 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA. , vol.96 , pp. 2662-2667
    • Malashkevich, V.N.1
  • 25
    • 84887847992 scopus 로고    scopus 로고
    • Structure and orientation study of Ebola fusion peptide inserted in lipid membrane models
    • 1838
    • Agopian, A., Castano, S. Structure and orientation study of Ebola fusion peptide inserted in lipid membrane models. Biochimica et Biophysica Acta (BBA)-Biomembranes 1838, 117-126 (2014).
    • (2014) Biochimica et Biophysica Acta (BBA)-Biomembranes , pp. 117-126
    • Agopian, A.1    Castano, S.2
  • 26
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissenhorn, W., Carfí, A., Lee, K., Skehel, J. J., Wiley, D. C. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol. Cell 2, 605-616 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 605-616
    • Weissenhorn, W.1    Carfí, A.2    Lee, K.3    Skehel, J.J.4    Wiley, D.C.5
  • 27
    • 39149137506 scopus 로고    scopus 로고
    • The creation of stable cell lines expressing Ebola virus glycoproteins and the matrix protein VP40 and generating Ebola virus-like particles utilizing an ecdysone inducible mammalian expression system
    • Melito, P. L., et al. The creation of stable cell lines expressing Ebola virus glycoproteins and the matrix protein VP40 and generating Ebola virus-like particles utilizing an ecdysone inducible mammalian expression system. J. Virol. Methods 148, 237-243 (2008).
    • (2008) J. Virol. Methods , vol.148 , pp. 237-243
    • Melito, P.L.1
  • 28
    • 84906346444 scopus 로고    scopus 로고
    • Spatial localization of the Ebola virus glycoprotein mucin-like domain determined by cryo-electron tomography
    • Tran, E. E., et al. Spatial localization of the Ebola virus glycoprotein mucin-like domain determined by cryo-electron tomography. J. Virol. 88, 10958-10962 (2014).
    • (2014) J. Virol. , vol.88 , pp. 10958-10962
    • Tran, E.E.1
  • 29
    • 84981180343 scopus 로고    scopus 로고
    • Mapping of Ebolavirus Neutralization by Monoclonal Antibodies in the ZMapp Cocktail Using Cryo-Electron Tomography and Studies of Cellular Entry
    • Tran, E. E., et al. Mapping of Ebolavirus Neutralization by Monoclonal Antibodies in the ZMapp Cocktail Using Cryo-Electron Tomography and Studies of Cellular Entry. J Virol. 90, 7618-7627 (2016).
    • (2016) J Virol. , vol.90 , pp. 7618-7627
    • Tran, E.E.1
  • 30
    • 37749007365 scopus 로고    scopus 로고
    • GraFix: Sample preparation for single-particle electron cryomicroscopy
    • Kastner, B., et al. GraFix: Sample preparation for single-particle electron cryomicroscopy. Nature methods 5, 53-55 (2008).
    • (2008) Nature Methods , vol.5 , pp. 53-55
    • Kastner, B.1
  • 31
    • 0028393194 scopus 로고
    • The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles
    • Penczek, P. A., Grassucci, R. A., Frank, J. The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles. Ultramicroscopy 53, 251-270 (1994).
    • (1994) Ultramicroscopy , vol.53 , pp. 251-270
    • Penczek, P.A.1    Grassucci, R.A.2    Frank, J.3
  • 32
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal P. B., Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol. 333, 721-745 (2003).
    • (2003) J Mol Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 33
    • 0029589329 scopus 로고
    • GP mRNA of Ebola Virus Is Edited by the Ebola Virus Polymerase and by T7 and Vaccinia Virus Polymerases 1
    • Volchkov, V. E., et al. GP mRNA of Ebola Virus Is Edited by the Ebola Virus Polymerase and by T7 and Vaccinia Virus Polymerases 1. Virology 214, 421-430 (1995).
    • (1995) Virology , vol.214 , pp. 421-430
    • Volchkov, V.E.1
  • 34
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • Henderson, R. The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. Q. Rev. Biophys. 28, 171-171 (1995).
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171
    • Henderson, R.1
  • 35
    • 84960797910 scopus 로고    scopus 로고
    • Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions
    • Zhao, Y., Ren, J., Harlos, K., Stuart, D. I. Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions. FEBS Lett (2016).
    • (2016) FEBS Lett
    • Zhao, Y.1    Ren, J.2    Harlos, K.3    Stuart, D.I.4
  • 36
    • 84969961924 scopus 로고    scopus 로고
    • Structural Insights into the Niemann-Pick C1 (NPC1)-Mediated Cholesterol Transfer and Ebola Infection
    • Gong, X., et al. Structural Insights into the Niemann-Pick C1 (NPC1)-Mediated Cholesterol Transfer and Ebola Infection. Cell. 165, 1467-1478 (2016).
    • (2016) Cell. , vol.165 , pp. 1467-1478
    • Gong, X.1
  • 37
    • 64049098349 scopus 로고    scopus 로고
    • Replication-deficient ebolavirus as a vaccine candidate
    • Halfmann, P., et al. Replication-deficient ebolavirus as a vaccine candidate. J. Virol. 83, 3810-3815 (2009).
    • (2009) J. Virol. , vol.83 , pp. 3810-3815
    • Halfmann, P.1
  • 38
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R., Chiu, W. EMAN: Semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 39
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., et al. SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1
  • 41
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F., et al. UCSF Chimera-a visualization system for exploratory research and analysis. Journal of computational chemistry. 25, 1605-1612 (2004).
    • (2004) Journal of Computational Chemistry , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


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