메뉴 건너뛰기




Volumn 24, Issue 2, 2018, Pages 441-452

Structural Definition of a Unique Neutralization Epitope on the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein

Author keywords

antibody epitope; coronavirus; crystal structure; Middle East respiratory syndrome; neutralizing antibody

Indexed keywords

CORONAVIRUS SPIKE GLYCOPROTEIN; DIPEPTIDYL PEPTIDASE IV; EPITOPE; NEUTRALIZING ANTIBODY; NEUTRALIZING ANTIBODY MERS 4; UNCLASSIFIED DRUG; PROTEIN BINDING;

EID: 85049315642     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2018.06.041     Document Type: Article
Times cited : (57)

References (53)
  • 4
    • 84867733836 scopus 로고    scopus 로고
    • Severe respiratory illness caused by a novel coronavirus, in a patient transferred to the United Kingdom from the Middle East, September 2012
    • Bermingham, A., Chand, M.A., Brown, C.S., Aarons, E., Tong, C., Langrish, C., Hoschler, K., Brown, K., Galiano, M., Myers, R., et al. Severe respiratory illness caused by a novel coronavirus, in a patient transferred to the United Kingdom from the Middle East, September 2012. Euro Surveill., 17, 2012, 20290.
    • (2012) Euro Surveill. , vol.17 , pp. 20290
    • Bermingham, A.1    Chand, M.A.2    Brown, C.S.3    Aarons, E.4    Tong, C.5    Langrish, C.6    Hoschler, K.7    Brown, K.8    Galiano, M.9    Myers, R.10
  • 6
    • 84886007720 scopus 로고    scopus 로고
    • Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus
    • Chen, Y., Rajashankar, K.R., Yang, Y., Agnihothram, S.S., Liu, C., Lin, Y.-L., Baric, R.S., Li, F., Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus. J. Virol. 87 (2013), 10777–10783.
    • (2013) J. Virol. , vol.87 , pp. 10777-10783
    • Chen, Y.1    Rajashankar, K.R.2    Yang, Y.3    Agnihothram, S.S.4    Liu, C.5    Lin, Y.-L.6    Baric, R.S.7    Li, F.8
  • 7
    • 85019596455 scopus 로고    scopus 로고
    • A novel neutralizing monoclonal antibody targeting the N-terminal domain of the MERS-CoV spike protein
    • Chen, Y., Lu, S., Jia, H., Deng, Y., Zhou, J., Huang, B., Yu, Y., Lan, J., Wang, W., Lou, Y., et al. A novel neutralizing monoclonal antibody targeting the N-terminal domain of the MERS-CoV spike protein. Emerg. Microbes Infect., 6, 2017, e37.
    • (2017) Emerg. Microbes Infect. , vol.6 , pp. e37
    • Chen, Y.1    Lu, S.2    Jia, H.3    Deng, Y.4    Zhou, J.5    Huang, B.6    Yu, Y.7    Lan, J.8    Wang, W.9    Lou, Y.10
  • 8
    • 85022339554 scopus 로고    scopus 로고
    • Human neutralizing monoclonal antibody inhibition of Middle East respiratory syndrome coronavirus replication in the common marmoset
    • Chen, Z., Bao, L., Chen, C., Zou, T., Xue, Y., Li, F., Lv, Q., Gu, S., Gao, X., Cui, S., et al. Human neutralizing monoclonal antibody inhibition of Middle East respiratory syndrome coronavirus replication in the common marmoset. J. Infect. Dis. 215 (2017), 1807–1815.
    • (2017) J. Infect. Dis. , vol.215 , pp. 1807-1815
    • Chen, Z.1    Bao, L.2    Chen, C.3    Zou, T.4    Xue, Y.5    Li, F.6    Lv, Q.7    Gu, S.8    Gao, X.9    Cui, S.10
  • 9
    • 84938854831 scopus 로고    scopus 로고
    • An outbreak of Middle East respiratory syndrome coronavirus infection in South Korea, 2015
    • Choi, J.Y., An outbreak of Middle East respiratory syndrome coronavirus infection in South Korea, 2015. Yonsei Med. J. 56 (2015), 1174–1176.
    • (2015) Yonsei Med. J. , vol.56 , pp. 1174-1176
    • Choi, J.Y.1
  • 10
    • 76549129820 scopus 로고    scopus 로고
    • Drug combination studies and their synergy quantification using the Chou-Talalay method
    • Chou, T.C., Drug combination studies and their synergy quantification using the Chou-Talalay method. Cancer Res. 70 (2010), 440–446.
    • (2010) Cancer Res. , vol.70 , pp. 440-446
    • Chou, T.C.1
  • 11
    • 0021118703 scopus 로고
    • Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors
    • Chou, T.C., Talalay, P., Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors. Adv. Enzyme Regul. 22 (1984), 27–55.
    • (1984) Adv. Enzyme Regul. , vol.22 , pp. 27-55
    • Chou, T.C.1    Talalay, P.2
  • 12
    • 84872694541 scopus 로고    scopus 로고
    • Implementation and performance of SIBYLS: a dual endstation small-angle X-ray scattering and macromolecular crystallography beamline at the Advanced Light Source
    • Classen, S., Hura, G.L., Holton, J.M., Rambo, R.P., Rodic, I., McGuire, P.J., Dyer, K., Hammel, M., Meigs, G., Frankel, K.A., Tainer, J.A., Implementation and performance of SIBYLS: a dual endstation small-angle X-ray scattering and macromolecular crystallography beamline at the Advanced Light Source. J. Appl. Cryst. 46 (2013), 1–13.
    • (2013) J. Appl. Cryst. , vol.46 , pp. 1-13
    • Classen, S.1    Hura, G.L.2    Holton, J.M.3    Rambo, R.P.4    Rodic, I.5    McGuire, P.J.6    Dyer, K.7    Hammel, M.8    Meigs, G.9    Frankel, K.A.10    Tainer, J.A.11
  • 15
    • 84901303550 scopus 로고    scopus 로고
    • A conformation-dependent neutralizing monoclonal antibody specifically targeting receptor-binding domain in Middle East respiratory syndrome coronavirus spike protein
    • Du, L., Zhao, G., Yang, Y., Qiu, H., Wang, L., Kou, Z., Tao, X., Yu, H., Sun, S., Tseng, C.T., et al. A conformation-dependent neutralizing monoclonal antibody specifically targeting receptor-binding domain in Middle East respiratory syndrome coronavirus spike protein. J. Virol. 88 (2014), 7045–7053.
    • (2014) J. Virol. , vol.88 , pp. 7045-7053
    • Du, L.1    Zhao, G.2    Yang, Y.3    Qiu, H.4    Wang, L.5    Kou, Z.6    Tao, X.7    Yu, H.8    Sun, S.9    Tseng, C.T.10
  • 16
  • 17
    • 84888011629 scopus 로고    scopus 로고
    • A decade after SARS: strategies for controlling emerging coronaviruses
    • Graham, R.L., Donaldson, E.F., Baric, R.S., A decade after SARS: strategies for controlling emerging coronaviruses. Nat. Rev. Microbiol. 11 (2013), 836–848.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 836-848
    • Graham, R.L.1    Donaldson, E.F.2    Baric, R.S.3
  • 18
    • 85007247657 scopus 로고    scopus 로고
    • Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding
    • Gui, M., Song, W., Zhou, H., Xu, J., Chen, S., Xiang, Y., Wang, X., Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding. Cell Res. 27 (2017), 119–129.
    • (2017) Cell Res. , vol.27 , pp. 119-129
    • Gui, M.1    Song, W.2    Zhou, H.3    Xu, J.4    Chen, S.5    Xiang, Y.6    Wang, X.7
  • 19
    • 0003519476 scopus 로고
    • Small Angle Scattering of X-rays
    • Wiley Interscience
    • Guinier, A., Fournet, F., Small Angle Scattering of X-rays. 1955, Wiley Interscience.
    • (1955)
    • Guinier, A.1    Fournet, F.2
  • 23
    • 84899797757 scopus 로고    scopus 로고
    • Potent neutralization of MERS-CoV by human neutralizing monoclonal antibodies to the viral spike glycoprotein
    • Jiang, L., Wang, N., Zuo, T., Shi, X., Poon, K.M., Wu, Y., Gao, F., Li, D., Wang, R., Guo, J., et al. Potent neutralization of MERS-CoV by human neutralizing monoclonal antibodies to the viral spike glycoprotein. Sci. Transl. Med., 6, 2014, 234ra59.
    • (2014) Sci. Transl. Med. , vol.6 , pp. 234ra59
    • Jiang, L.1    Wang, N.2    Zuo, T.3    Shi, X.4    Poon, K.M.5    Wu, Y.6    Gao, F.7    Li, D.8    Wang, R.9    Guo, J.10
  • 24
    • 84871990813 scopus 로고    scopus 로고
    • Cooperativity in virus neutralization by human monoclonal antibodies to two adjacent regions located at the amino terminus of hepatitis C virus E2 glycoprotein
    • Keck, Z., Wang, W., Wang, Y., Lau, P., Carlsen, T.H., Prentoe, J., Xia, J., Patel, A.H., Bukh, J., Foung, S.K., Cooperativity in virus neutralization by human monoclonal antibodies to two adjacent regions located at the amino terminus of hepatitis C virus E2 glycoprotein. J. Virol. 87 (2013), 37–51.
    • (2013) J. Virol. , vol.87 , pp. 37-51
    • Keck, Z.1    Wang, W.2    Wang, Y.3    Lau, P.4    Carlsen, T.H.5    Prentoe, J.6    Xia, J.7    Patel, A.H.8    Bukh, J.9    Foung, S.K.10
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993), 283–291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 84946491594 scopus 로고    scopus 로고
    • A humanized neutralizing antibody against MERS-CoV targeting the receptor-binding domain of the spike protein
    • Li, Y., Wan, Y., Liu, P., Zhao, J., Lu, G., Qi, J., Wang, Q., Lu, X., Wu, Y., Liu, W., et al. A humanized neutralizing antibody against MERS-CoV targeting the receptor-binding domain of the spike protein. Cell Res. 25 (2015), 1237–1249.
    • (2015) Cell Res. , vol.25 , pp. 1237-1249
    • Li, Y.1    Wan, Y.2    Liu, P.3    Zhao, J.4    Lu, G.5    Qi, J.6    Wang, Q.7    Lu, X.8    Wu, Y.9    Liu, W.10
  • 27
    • 84881479703 scopus 로고    scopus 로고
    • Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26
    • Lu, G., Hu, Y., Wang, Q., Qi, J., Gao, F., Li, Y., Zhang, Y., Zhang, W., Yuan, Y., Bao, J., et al. Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26. Nature 500 (2013), 227–231.
    • (2013) Nature , vol.500 , pp. 227-231
    • Lu, G.1    Hu, Y.2    Wang, Q.3    Qi, J.4    Gao, F.5    Li, Y.6    Zhang, Y.7    Zhang, W.8    Yuan, Y.9    Bao, J.10
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997), 307–326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 10944238037 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome
    • Peiris, J.S., Guan, Y., Yuen, K.Y., Severe acute respiratory syndrome. Nat. Med. 10:Suppl 12 (2004), S88–S97.
    • (2004) Nat. Med. , vol.10 , pp. S88-S97
    • Peiris, J.S.1    Guan, Y.2    Yuen, K.Y.3
  • 35
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle X-ray scattering
    • Pelikan, M., Hura, G.L., Hammel, M., Structure and flexibility within proteins as identified through small angle X-ray scattering. Gen. Physiol. Biophys. 28 (2009), 174–189.
    • (2009) Gen. Physiol. Biophys. , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 37
    • 84975503800 scopus 로고    scopus 로고
    • Epitope-focused vaccine design against influenza A and B viruses
    • Ren, H., Zhou, P., Epitope-focused vaccine design against influenza A and B viruses. Curr. Opin. Immunol. 42 (2016), 83–90.
    • (2016) Curr. Opin. Immunol. , vol.42 , pp. 83-90
    • Ren, H.1    Zhou, P.2
  • 38
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A., Blundell, T.L., Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993), 779–815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 39
    • 84882940564 scopus 로고    scopus 로고
    • Accurate SAXS profile computation and its assessment by contrast variation experiments
    • Schneidman-Duhovny, D., Hammel, M., Tainer, J.A., Sali, A., Accurate SAXS profile computation and its assessment by contrast variation experiments. Biophys. J. 105 (2013), 962–974.
    • (2013) Biophys. J. , vol.105 , pp. 962-974
    • Schneidman-Duhovny, D.1    Hammel, M.2    Tainer, J.A.3    Sali, A.4
  • 40
    • 85013011986 scopus 로고    scopus 로고
    • FoXS, FoXSDock and MultiFoXS: single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles
    • Schneidman-Duhovny, D., Hammel, M., Tainer, J.A., Sali, A., FoXS, FoXSDock and MultiFoXS: single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles. Nucleic Acids Res. 44:W1 (2016), W424–W429.
    • (2016) Nucleic Acids Res. , vol.44 , Issue.W1 , pp. W424-W429
    • Schneidman-Duhovny, D.1    Hammel, M.2    Tainer, J.A.3    Sali, A.4
  • 41
    • 79954589594 scopus 로고    scopus 로고
    • Genetic and neutralization sensitivity of diverse HIV-1 env clones from chronically infected patients in China
    • Shang, H., Han, X., Shi, X., Zuo, T., Goldin, M., Chen, D., Han, B., Sun, W., Wu, H., Wang, X., Zhang, L., Genetic and neutralization sensitivity of diverse HIV-1 env clones from chronically infected patients in China. J. Biol. Chem. 286 (2011), 14531–14541.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14531-14541
    • Shang, H.1    Han, X.2    Shi, X.3    Zuo, T.4    Goldin, M.5    Chen, D.6    Han, B.7    Sun, W.8    Wu, H.9    Wang, X.10    Zhang, L.11
  • 43
    • 84881190964 scopus 로고    scopus 로고
    • Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4
    • Wang, N., Shi, X., Jiang, L., Zhang, S., Wang, D., Tong, P., Guo, D., Fu, L., Cui, Y., Liu, X., et al. Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4. Cell Res. 23 (2013), 986–993.
    • (2013) Cell Res. , vol.23 , pp. 986-993
    • Wang, N.1    Shi, X.2    Jiang, L.3    Zhang, S.4    Wang, D.5    Tong, P.6    Guo, D.7    Fu, L.8    Cui, Y.9    Liu, X.10
  • 46
    • 85046008693 scopus 로고    scopus 로고
    • Importance of neutralizing monoclonal antibodies targeting multiple antigenic sites on MERS-CoV Spike to avoid neutralization escape
    • e02002-17
    • Wang, L., Shi, W., Chappell, J.D., Joyce, M.G., Zhang, Y., Kanekiyo, M., Becker, M.M., van Doremalen, N., Fischer, R., Wang, N., et al. Importance of neutralizing monoclonal antibodies targeting multiple antigenic sites on MERS-CoV Spike to avoid neutralization escape. J. Virol., 92, 2018 e02002-17.
    • (2018) J. Virol. , vol.92
    • Wang, L.1    Shi, W.2    Chappell, J.D.3    Joyce, M.G.4    Zhang, Y.5    Kanekiyo, M.6    Becker, M.M.7    van Doremalen, N.8    Fischer, R.9    Wang, N.10
  • 47
    • 84973307903 scopus 로고    scopus 로고
    • Antigenic landscape of the HIV-1 envelope and new immunological concepts defined by HIV-1 broadly neutralizing antibodies
    • Wu, X., Kong, X.P., Antigenic landscape of the HIV-1 envelope and new immunological concepts defined by HIV-1 broadly neutralizing antibodies. Curr. Opin. Immunol. 42 (2016), 56–64.
    • (2016) Curr. Opin. Immunol. , vol.42 , pp. 56-64
    • Wu, X.1    Kong, X.P.2
  • 48
    • 84904663317 scopus 로고    scopus 로고
    • Exceptionally potent neutralization of Middle East respiratory syndrome coronavirus by human monoclonal antibodies
    • Ying, T., Du, L., Ju, T.W., Prabakaran, P., Lau, C.C., Lu, L., Liu, Q., Wang, L., Feng, Y., Wang, Y., et al. Exceptionally potent neutralization of Middle East respiratory syndrome coronavirus by human monoclonal antibodies. J. Virol. 88 (2014), 7796–7805.
    • (2014) J. Virol. , vol.88 , pp. 7796-7805
    • Ying, T.1    Du, L.2    Ju, T.W.3    Prabakaran, P.4    Lau, C.C.5    Lu, L.6    Liu, Q.7    Wang, L.8    Feng, Y.9    Wang, Y.10
  • 49
    • 84941788522 scopus 로고    scopus 로고
    • Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody
    • Ying, T., Prabakaran, P., Du, L., Shi, W., Feng, Y., Wang, Y., Wang, L., Li, W., Jiang, S., Dimitrov, D.S., Zhou, T., Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody. Nat. Commun., 6, 2015, 8223.
    • (2015) Nat. Commun. , vol.6 , pp. 8223
    • Ying, T.1    Prabakaran, P.2    Du, L.3    Shi, W.4    Feng, Y.5    Wang, Y.6    Wang, L.7    Li, W.8    Jiang, S.9    Dimitrov, D.S.10    Zhou, T.11
  • 50
    • 84939545662 scopus 로고    scopus 로고
    • Structural basis for the neutralization of MERS-CoV by a human monoclonal antibody MERS-27
    • Yu, X., Zhang, S., Jiang, L., Cui, Y., Li, D., Wang, D., Wang, N., Fu, L., Shi, X., Li, Z., et al. Structural basis for the neutralization of MERS-CoV by a human monoclonal antibody MERS-27. Sci. Rep., 5, 2015, 13133.
    • (2015) Sci. Rep. , vol.5 , pp. 13133
    • Yu, X.1    Zhang, S.2    Jiang, L.3    Cui, Y.4    Li, D.5    Wang, D.6    Wang, N.7    Fu, L.8    Shi, X.9    Li, Z.10
  • 51
    • 85017378927 scopus 로고    scopus 로고
    • Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains
    • Yuan, Y., Cao, D., Zhang, Y., Ma, J., Qi, J., Wang, Q., Lu, G., Wu, Y., Yan, J., Shi, Y., et al. Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains. Nat. Commun., 8, 2017, 15092.
    • (2017) Nat. Commun. , vol.8 , pp. 15092
    • Yuan, Y.1    Cao, D.2    Zhang, Y.3    Ma, J.4    Qi, J.5    Wang, Q.6    Lu, G.7    Wu, Y.8    Yan, J.9    Shi, Y.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.