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Volumn 3, Issue 6, 2018, Pages 670-677

Broadly neutralizing antibodies from human survivors target a conserved site in the ebola virus glycoprotein hr2-mper region

(24)  Flyak, Andrew I a,g   Kuzmina, Natalia b,c   Murin, Charles D d   Bryan, Christopher e   Davidson, Edgar e   Gilchuk, Pavlo f   Gulka, Christopher P f   Ilinykh, Philipp A b,c   Shen, Xiaoli b,c   Huang, Kai b,c   Ramanathan, Palaniappan b,c   Turner, Hannah d   Fusco, Marnie L d   Lampley, Rebecca f   Kose, Nurgun f   King, Hannah f   Sapparapu, Gopal f   Doranz, Benjamin J e   Ksiazek, Thomas G b,c   Wright, David W f   more..


Author keywords

[No Author keywords available]

Indexed keywords

EBOLA VACCINE; EPITOPE; NEUTRALIZING ANTIBODY; PEPTIDE; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; VIRUS GLYCOPROTEIN HR2 MPER; MEMBRANE PROTEIN; PROTEIN BINDING; VIRAL PROTEIN; VIRUS ANTIBODY;

EID: 85046541781     PISSN: None     EISSN: 20585276     Source Type: Journal    
DOI: 10.1038/s41564-018-0157-z     Document Type: Article
Times cited : (65)

References (41)
  • 1
    • 84907263545 scopus 로고    scopus 로고
    • Reversion of advanced ebola virus disease in nonhuman primates with zmapp
    • Qiu, X. et al. Reversion of advanced Ebola virus disease in nonhuman primates with ZMapp. Nature 514, 47-53 (2014).
    • (2014) Nature , vol.514 , pp. 47-53
    • Qiu, X.1
  • 2
    • 84912539210 scopus 로고    scopus 로고
    • Clinical care of two patients with ebola virus disease in the United States
    • Lyon, G. M. et al. Clinical care of two patients with Ebola virus disease in the United States. N. Engl. J. Med. 371, 2402-2409 (2014).
    • (2014) N. Engl. J. Med. , vol.371 , pp. 2402-2409
    • Lyon, G.M.1
  • 3
    • 80054837546 scopus 로고    scopus 로고
    • Characterization of Zaire ebolavirus glycoprotein-specific monoclonal antibodies
    • Qiu, X. et al. Characterization of Zaire ebolavirus glycoprotein-specific monoclonal antibodies. Clin. Immunol. 141, 218-227 (2011).
    • (2011) Clin. Immunol. , vol.141 , pp. 218-227
    • Qiu, X.1
  • 4
    • 84862525229 scopus 로고    scopus 로고
    • Successful treatment of ebola virus-infected cynomolgus macaques with monoclonal antibodies
    • Qiu, X. et al. Successful treatment of Ebola virus-infected cynomolgus macaques with monoclonal antibodies. Sci. Transl. Med. 4, 138ra81 (2012).
    • (2012) Sci. Transl. Med. , vol.4 , pp. 138ra81
    • Qiu, X.1
  • 5
    • 84868149422 scopus 로고    scopus 로고
    • Delayed treatment of ebola virus infection with plant-derived monoclonal antibodies provides protection in rhesus macaques
    • Olinger, G. G. Jr et al. Delayed treatment of Ebola virus infection with plant-derived monoclonal antibodies provides protection in rhesus macaques. Proc. Natl Acad. Sci. USA 109, 18030-18035 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 18030-18035
    • Olinger, G.G.1
  • 6
    • 0034051595 scopus 로고    scopus 로고
    • Epitopes involved in antibody-mediated protection from ebola virus
    • Wilson, J. A. et al. Epitopes involved in antibody-mediated protection from Ebola virus. Science 287, 1664-1666 (2000).
    • (2000) Science , vol.287 , pp. 1664-1666
    • Wilson, J.A.1
  • 7
    • 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
  • 8
    • 84945217199 scopus 로고    scopus 로고
    • Mechanism of binding to ebola virus glycoprotein by the zmapp, zmab, and mb-003 cocktail antibodies
    • Davidson, E. et al. Mechanism of binding to Ebola virus glycoprotein by the ZMapp, ZMAb, and MB-003 cocktail antibodies. J. Virol. 89, 10982-10992 (2015).
    • (2015) J. Virol. , vol.89 , pp. 10982-10992
    • Davidson, E.1
  • 9
    • 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
  • 10
    • 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
  • 11
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the ebola virus membrane fusion subunit, gp2, from the envelope glycoprotein ectodomain
    • Weissenhorn, W., Carfi, A., Lee, K. H., 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    Carfi, A.2    Lee, K.H.3    Skehel, J.J.4    Wiley, D.C.5
  • 12
    • 84960400876 scopus 로고    scopus 로고
    • Isolation of potent neutralizing antibodies from a survivor of the 2014 ebola virus outbreak
    • Bornholdt, Z. A. et al. Isolation of potent neutralizing antibodies from a survivor of the 2014 Ebola virus outbreak. Science 351, 1078-1083 (2016).
    • (2016) Science , vol.351 , pp. 1078-1083
    • Bornholdt, Z.A.1
  • 13
    • 85019578866 scopus 로고    scopus 로고
    • Antibodies from a human survivor define sites of vulnerability for broad protection against ebolaviruses
    • Wec, A. Z. et al. Antibodies from a human survivor define sites of vulnerability for broad protection against ebolaviruses. Cell 169, 878-890 (2017).
    • (2017) Cell , vol.169 , pp. 878-890
    • Wec, A.Z.1
  • 14
    • 33748705342 scopus 로고    scopus 로고
    • Detection of ebola virus envelope using monoclonal and polyclonal antibodies in elisa, surface plasmon resonance and a quartz crystal microbalance immunosensor
    • Yu, J. S. et al. Detection of Ebola virus envelope using monoclonal and polyclonal antibodies in ELISA, surface plasmon resonance and a quartz crystal microbalance immunosensor. J. Virol. Methods 137, 219-228 (2006).
    • (2006) J. Virol. Methods , vol.137 , pp. 219-228
    • Yu, J.S.1
  • 15
    • 84988962295 scopus 로고    scopus 로고
    • The domestic ferret (mustela putorius furo) as a lethal infection model for 3 species of Ebolavirus
    • Cross, R. W. et al. The domestic ferret (Mustela putorius furo) as a lethal infection model for 3 species of Ebolavirus. J. Infect. Dis. 214, 565-569 (2016).
    • (2016) J. Infect. Dis. , vol.214 , pp. 565-569
    • Cross, R.W.1
  • 16
    • 84990052916 scopus 로고    scopus 로고
    • Ferrets infected with bundibugyo virus or ebola virus recapitulate important aspects of human filovirus disease
    • Kozak, R. et al. Ferrets infected with Bundibugyo virus or Ebola virus recapitulate important aspects of human filovirus disease. J. Virol. 90, 9209-9223 (2016).
    • (2016) J. Virol. , vol.90 , pp. 9209-9223
    • Kozak, R.1
  • 17
    • 84963838685 scopus 로고    scopus 로고
    • Chimeric filoviruses for identification and characterization of monoclonal antibodies
    • Ilinykh, P. A. et al. Chimeric filoviruses for identification and characterization of monoclonal antibodies. J. Virol. 90, 3890-3901 (2016).
    • (2016) J. Virol. , vol.90 , pp. 3890-3901
    • Ilinykh, P.A.1
  • 18
    • 0033020204 scopus 로고    scopus 로고
    • Core structure of the envelope glycoprotein gp2 from ebola virus at 1.9-Å resolution
    • Malashkevich, V. N. et al. Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-Å 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
  • 19
    • 85029567578 scopus 로고    scopus 로고
    • Structure of the ebola virus envelope protein mper/tm domain and its interaction with the fusion loop explains their fusion activity
    • Lee, J. et al. Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity. Proc. Natl Acad. Sci. USA 114, E7987-E7996 (2017).
    • (2017) Proc. Natl Acad. Sci. USA , vol.114 , pp. E7987-E7996
    • Lee, J.1
  • 20
    • 85019650530 scopus 로고    scopus 로고
    • Immunization-elicited broadly protective antibody reveals ebolavirus fusion loop as a site of vulnerability
    • Zhao, X. et al. Immunization-elicited broadly protective antibody reveals ebolavirus fusion loop as a site of vulnerability. Cell 169, 891-904 (2017).
    • (2017) Cell , vol.169 , pp. 891-904
    • Zhao, X.1
  • 21
    • 0027378573 scopus 로고
    • A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1
    • Muster, T. et al. A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J. Virol. 67, 6642-6647 (1993).
    • (1993) J. Virol. , vol.67 , pp. 6642-6647
    • Muster, T.1
  • 22
    • 0034759882 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41
    • Zwick, M. B. et al. Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J. Virol. 75, 10892-10905 (2001).
    • (2001) J. Virol. , vol.75 , pp. 10892-10905
    • Zwick, M.B.1
  • 23
    • 40849136223 scopus 로고    scopus 로고
    • The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: Dominant site of antibody neutralization and target for vaccine design
    • Montero, M., van Houten, N. E., Wang, X. & Scott, J. K. The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design. Microbiol. Mol. Biol. Rev. 72, 54-84 (2008).
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 54-84
    • Montero, M.1    Van Houten, N.E.2    Wang, X.3    Scott, J.K.4
  • 24
    • 64849114224 scopus 로고    scopus 로고
    • Antibody recognition of a highly conserved influenza virus epitope
    • Ekiert, D. C. et al. Antibody recognition of a highly conserved influenza virus epitope. Science 324, 246-251 (2009).
    • (2009) Science , vol.324 , pp. 246-251
    • Ekiert, D.C.1
  • 25
    • 62049083943 scopus 로고    scopus 로고
    • Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
    • Sui, J. et al. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nat. Struct. Mol. Biol. 16, 265-273 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 265-273
    • Sui, J.1
  • 26
    • 80051670323 scopus 로고    scopus 로고
    • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins
    • Corti, D. et al. A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 333, 850-856 (2011).
    • (2011) Science , vol.333 , pp. 850-856
    • Corti, D.1
  • 27
    • 84923366926 scopus 로고    scopus 로고
    • Mechanism of human antibody-mediated neutralization of Marburg virus
    • Flyak, A. I. et al. Mechanism of human antibody-mediated neutralization of Marburg virus. Cell 160, 893-903 (2015).
    • (2015) Cell , vol.160 , pp. 893-903
    • Flyak, A.I.1
  • 28
    • 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
  • 29
    • 73349143321 scopus 로고    scopus 로고
    • Techniques and tactics used in determining the structure of the trimeric ebolavirus glycoprotein
    • Lee, J. E. et al. Techniques and tactics used in determining the structure of the trimeric ebolavirus glycoprotein. Acta Crystallogr. D Biol. Crystallogr. 65, 1162-1180 (2009).
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 1162-1180
    • Lee, J.E.1
  • 30
    • 12344297305 scopus 로고    scopus 로고
    • Generation of egfp expressing recombinant zaire ebolavirus for analysis of early pathogenesis events and high-Throughput antiviral drug screening
    • Towner, J. S. et al. Generation of eGFP expressing recombinant Zaire ebolavirus for analysis of early pathogenesis events and high-Throughput antiviral drug screening. Virology 332, 20-27 (2005).
    • (2005) Virology , vol.332 , pp. 20-27
    • Towner, J.S.1
  • 31
    • 84880347654 scopus 로고    scopus 로고
    • The lack of maturation of ebola virus-infected dendritic cells results from the cooperative effect of at least two viral domains
    • Lubaki, N. M. et al. The lack of maturation of Ebola virus-infected dendritic cells results from the cooperative effect of at least two viral domains. J. Virol. 87, 7471-7485 (2013).
    • (2013) J. Virol. , vol.87 , pp. 7471-7485
    • Lubaki, N.M.1
  • 32
    • 20544468931 scopus 로고    scopus 로고
    • Automated molecular microscopy: The new leginon system
    • Suloway, C. et al. Automated molecular microscopy: The new Leginon system. J. Struct. Biol. 151, 41-60 (2005).
    • (2005) J. Struct. Biol. , vol.151 , pp. 41-60
    • Suloway, C.1
  • 33
    • 60649103238 scopus 로고    scopus 로고
    • Appion: An integrated, database-driven pipeline to facilitate em image processing
    • Lander, G. C. et al. Appion: An integrated, database-driven pipeline to facilitate EM image processing. J. Struct. Biol. 166, 95-102 (2009).
    • (2009) J. Struct. Biol. , vol.166 , pp. 95-102
    • Lander, G.C.1
  • 34
    • 63649113687 scopus 로고    scopus 로고
    • Dog picker and tiltpicker: Software tools to facilitate particle selection in single particle electron microscopy
    • Voss, N. R., Yoshioka, C. K., Radermacher, M., Potter, C. S. & Carragher, B. DoG Picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy. J. Struct. Biol. 166, 205-213 (2009).
    • (2009) J. Struct. Biol. , vol.166 , pp. 205-213
    • Voss, N.R.1    Yoshioka, C.K.2    Radermacher, M.3    Potter, C.S.4    Carragher, B.5
  • 36
    • 84904868707 scopus 로고    scopus 로고
    • A high-Throughput shotgun mutagenesis approach to mapping b-cell antibody epitopes
    • Davidson, E. & Doranz, B. J. A high-Throughput shotgun mutagenesis approach to mapping B-cell antibody epitopes. Immunology 143, 13-20 (2014).
    • (2014) Immunology , vol.143 , pp. 13-20
    • Davidson, E.1    Doranz, B.J.2
  • 39
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields, G. B. & Noble, R. L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int J. Pept. Protein Res. 35, 161-214 (1990).
    • (1990) Int J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 40
    • 0024729231 scopus 로고
    • Synthesis of peptide amides by fmoc-solid-phase peptide synthesis and acid labile anchor groups
    • Stuber, W., Knolle, J. & Breipohl, G. Synthesis of peptide amides by Fmoc-solid-phase peptide synthesis and acid labile anchor groups. Int J. Pept. Protein Res. 34, 215-221 (1989).
    • (1989) Int J. Pept. Protein Res. , vol.34 , pp. 215-221
    • Stuber, W.1    Knolle, J.2    Breipohl, G.3
  • 41
    • 0001311689 scopus 로고
    • Peptide synthesis: Part 10. Use of pentafluorophenyl esters of fluorenylmethoxycarbonyl amino acids in solid phase peptide synthesis
    • Atherton, E., Cameron, L. R. & Sheppard, R. C. Peptide synthesis: part 10. Use of pentafluorophenyl esters of fluorenylmethoxycarbonyl amino acids in solid phase peptide synthesis. Tetrahedron 44, 843-857 (1988).
    • (1988) Tetrahedron , vol.44 , pp. 843-857
    • Atherton, E.1    Cameron, L.R.2    Sheppard, R.C.3


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