메뉴 건너뛰기




Volumn 531, Issue 7592, 2016, Pages 114-117

Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer

Author keywords

[No Author keywords available]

Indexed keywords

CORONAVIRUS SPIKE GLYCOPROTEIN; F PROTEIN; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; VIRUS FUSION PROTEIN; VIRUS PROTEIN; VIRUS VACCINE;

EID: 84960090603     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature16988     Document Type: Article
Times cited : (403)

References (53)
  • 1
    • 60749134643 scopus 로고    scopus 로고
    • The spike protein of SARS-CoV-A target for vaccine and therapeutic development
    • Du, L. et al. The spike protein of SARS-CoV-a target for vaccine and therapeutic development. Nature Rev. Microbiol. 7, 226-236 (2009).
    • (2009) Nature Rev. Microbiol. , vol.7 , pp. 226-236
    • Du, L.1
  • 2
    • 84878349946 scopus 로고    scopus 로고
    • Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody
    • McLellan, J. S. et al. Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody. Science 340, 1113-1117 (2013).
    • (2013) Science , vol.340 , pp. 1113-1117
    • McLellan, J.S.1
  • 3
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin, H. S., Wen, X., Paterson, R. G., Lamb, R. A. & Jardetzky, T. S. Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439, 38-44 (2006).
    • (2006) Nature , vol.439 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 4
    • 84899122287 scopus 로고    scopus 로고
    • Coronaviruses: Important emerging human pathogens
    • Coleman, C. M. & Frieman, M. B. Coronaviruses: important emerging human pathogens. J. Virol. 88, 5209-5212 (2014).
    • (2014) J. Virol. , vol.88 , pp. 5209-5212
    • Coleman, C.M.1    Frieman, M.B.2
  • 5
    • 0042208243 scopus 로고    scopus 로고
    • The coronavirus spike protein is a class I virus fusion protein: Structural and functional characterization of the fusion core complex
    • Bosch, B. J., van der Zee, R., de Haan, C. A. & Rottier, P. J. The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex. J. Virol. 77, 8801-8811 (2003).
    • (2003) J. Virol. , vol.77 , pp. 8801-8811
    • Bosch, B.J.1    Van Der-Zee, R.2    De Haan, C.A.3    Rottier, P.J.4
  • 6
    • 84912120721 scopus 로고    scopus 로고
    • Coronavirus cell entry occurs through the endo-/lysosomal pathway in a proteolysis-dependent manner
    • Burkard, C. et al. Coronavirus cell entry occurs through the endo-/lysosomal pathway in a proteolysis-dependent manner. PLoS Pathog. 10, e1004502 (2014).
    • (2014) PLoS Pathog. , vol.10 , pp. e1004502
    • Burkard, C.1
  • 7
    • 3142663245 scopus 로고    scopus 로고
    • Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core
    • Xu, Y. et al. Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core. J. Biol. Chem. 279, 30514-30522 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 30514-30522
    • Xu, Y.1
  • 8
    • 17444401009 scopus 로고    scopus 로고
    • Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein
    • Duquerroy, S., Vigouroux, A., Rottier, P. J., Rey, F. A. & Bosch, B. J. Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein. Virology 335, 276-285 (2005).
    • (2005) Virology , vol.335 , pp. 276-285
    • Duquerroy, S.1    Vigouroux, A.2    Rottier, P.J.3    Rey, F.A.4    Bosch, B.J.5
  • 9
    • 84888052193 scopus 로고    scopus 로고
    • Structure of the fusion core and inhibition of fusion by a heptad repeat peptide derived from the S protein of Middle East respiratory syndrome coronavirus
    • Gao, J. et al. Structure of the fusion core and inhibition of fusion by a heptad repeat peptide derived from the S protein of Middle East respiratory syndrome coronavirus. J. Virol. 87, 13134-13140 (2013).
    • (2013) J. Virol. , vol.87 , pp. 13134-13140
    • Gao, J.1
  • 10
    • 11144237311 scopus 로고    scopus 로고
    • Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein
    • Supekar, V. M. et al. Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein. Proc. Natl Acad. Sci. USA 101, 17958-17963 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 17958-17963
    • Supekar, V.M.1
  • 11
    • 84881479703 scopus 로고    scopus 로고
    • Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26
    • Lu, G. et al. Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26. Nature 500, 227-231 (2013).
    • (2013) Nature , vol.500 , pp. 227-231
    • Lu, G.1
  • 12
    • 24944498409 scopus 로고    scopus 로고
    • Structure of SARS coronavirus spike receptor-binding domain complexed with receptor
    • Li, F., Li, W., Farzan, M. & Harrison, S. C. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science 309, 1864-1868 (2005).
    • (2005) Science , vol.309 , pp. 1864-1868
    • Li, F.1    Li, W.2    Farzan, M.3    Harrison, S.C.4
  • 13
    • 79960567167 scopus 로고    scopus 로고
    • Crystal structure of mouse coronavirus receptor-binding domain complexed with its murine receptor
    • Peng, G. et al. Crystal structure of mouse coronavirus receptor-binding domain complexed with its murine receptor. Proc. Natl Acad. Sci. USA 108, 10696-10701 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 10696-10701
    • Peng, G.1
  • 14
    • 73949110051 scopus 로고    scopus 로고
    • Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor
    • Wu, K., Li, W., Peng, G. & Li, F. Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor. Proc. Natl Acad. Sci. USA 106, 19970-19974 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 19970-19974
    • Wu, K.1    Li, W.2    Peng, G.3    Li, F.4
  • 16
    • 84928400353 scopus 로고    scopus 로고
    • Single-particle cryo-EM at crystallographic resolution
    • Cheng, Y. Single-particle cryo-EM at crystallographic resolution. Cell 161, 450-457 (2015).
    • (2015) Cell , vol.161 , pp. 450-457
    • Cheng, Y.1
  • 17
    • 84871290676 scopus 로고    scopus 로고
    • Crystal structure of bovine coronavirus spike protein lectin domain
    • Peng, G. et al. Crystal structure of bovine coronavirus spike protein lectin domain. J. Biol. Chem. 287, 41931-41938 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 41931-41938
    • Peng, G.1
  • 18
    • 84921777915 scopus 로고    scopus 로고
    • Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
    • Brown, A. et al. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D 71, 136-153 (2015).
    • (2015) Acta Crystallogr. D , vol.71 , pp. 136-153
    • Brown, A.1
  • 19
    • 84926520440 scopus 로고    scopus 로고
    • Atomic-accuracy models from 4.5-A cryo-electron microscopy data with density-guided iterative local refinement
    • DiMaio, F. et al. Atomic-accuracy models from 4.5-A cryo-electron microscopy data with density-guided iterative local refinement. Nature Methods 12, 361-365 (2015).
    • (2015) Nature Methods , vol.12 , pp. 361-365
    • DiMaio, F.1
  • 20
    • 84926516252 scopus 로고    scopus 로고
    • De novo protein structure determination from near-atomicresolution cryo-EM maps
    • Wang, R. Y. et al. De novo protein structure determination from near-atomicresolution cryo-EM maps. Nature Methods 12, 335-338 (2015).
    • (2015) Nature Methods , vol.12 , pp. 335-338
    • Wang, R.Y.1
  • 21
    • 0035129841 scopus 로고    scopus 로고
    • Variations in disparate regions of the murine coronavirus spike protein impact the initiation of membrane fusion
    • Krueger, D. K., Kelly, S. M., Lewicki, D. N., Ruffolo, R. & Gallagher, T. M. Variations in disparate regions of the murine coronavirus spike protein impact the initiation of membrane fusion. J. Virol. 75, 2792-2802 (2001).
    • (2001) J. Virol. , vol.75 , pp. 2792-2802
    • Krueger, D.K.1    Kelly, S.M.2    Lewicki, D.N.3    Ruffolo, R.4    Gallagher, T.M.5
  • 22
    • 0036147337 scopus 로고    scopus 로고
    • Soluble receptor potentiates receptor-independent infection by murine coronavirus
    • Taguchi, F. & Matsuyama, S. Soluble receptor potentiates receptor-independent infection by murine coronavirus. J. Virol. 76, 950-958 (2002).
    • (2002) J. Virol. , vol.76 , pp. 950-958
    • Taguchi, F.1    Matsuyama, S.2
  • 23
    • 67650899039 scopus 로고    scopus 로고
    • Characterization of a highly conserved domain within the severe acute respiratory syndrome coronavirus spike protein S2 domain with characteristics of a viral fusion peptide
    • Madu, I. G., Roth, S. L., Belouzard, S. & Whittaker, G. R. Characterization of a highly conserved domain within the severe acute respiratory syndrome coronavirus spike protein S2 domain with characteristics of a viral fusion peptide. J. Virol. 83, 7411-7421 (2009).
    • (2009) J. Virol. , vol.83 , pp. 7411-7421
    • Madu, I.G.1    Roth, S.L.2    Belouzard, S.3    Whittaker, G.R.4
  • 24
    • 84904637027 scopus 로고    scopus 로고
    • Proteolytic activation of the porcine epidemic diarrhea coronavirus spike fusion protein by trypsin in cell culture
    • Wicht, O. et al. Proteolytic activation of the porcine epidemic diarrhea coronavirus spike fusion protein by trypsin in cell culture. J. Virol. 88, 7952-7961 (2014).
    • (2014) J. Virol. , vol.88 , pp. 7952-7961
    • Wicht, O.1
  • 25
    • 84909640954 scopus 로고    scopus 로고
    • Structure and immune recognition of trimeric pre-fusion HIV-1 Env
    • Pancera, M. et al. Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Nature 514, 455-461 (2014).
    • (2014) Nature , vol.514 , pp. 455-461
    • Pancera, M.1
  • 26
    • 0027400766 scopus 로고
    • Identification of an immunodominant linear neutralization domain on the S2 portion of the murine coronavirus spike glycoprotein and evidence that it forms part of complex tridimensional structure
    • Daniel, C. et al. Identification of an immunodominant linear neutralization domain on the S2 portion of the murine coronavirus spike glycoprotein and evidence that it forms part of complex tridimensional structure. J. Virol. 67, 1185-1194 (1993).
    • (1993) J. Virol. , vol.67 , pp. 1185-1194
    • Daniel, C.1
  • 27
    • 2942647919 scopus 로고    scopus 로고
    • Identification of an antigenic determinant on the S2 domain of the severe acute respiratory syndrome coronavirus spike glycoprotein capable of inducing neutralizing antibodies
    • Zhang, H. et al. Identification of an antigenic determinant on the S2 domain of the severe acute respiratory syndrome coronavirus spike glycoprotein capable of inducing neutralizing antibodies. J. Virol. 78, 6938-6945 (2004).
    • (2004) J. Virol. , vol.78 , pp. 6938-6945
    • Zhang, H.1
  • 28
    • 84896315237 scopus 로고    scopus 로고
    • Proof of principle for epitope-focused vaccine design
    • Correia, B. E. et al. Proof of principle for epitope-focused vaccine design. Nature 507, 201-206 (2014).
    • (2014) Nature , vol.507 , pp. 201-206
    • Correia, B.E.1
  • 29
    • 84907681989 scopus 로고    scopus 로고
    • Bat origins of MERS-CoV supported by bat coronavirus HKU4 usage of human receptor CD26
    • Wang, Q. et al. Bat origins of MERS-CoV supported by bat coronavirus HKU4 usage of human receptor CD26. Cell Host Microbe 16, 328-337 (2014).
    • (2014) Cell Host Microbe , vol.16 , pp. 328-337
    • Wang, Q.1
  • 30
    • 84866168715 scopus 로고    scopus 로고
    • Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies
    • Reguera, J. et al. Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies. PLoS Pathog. 8, e1002859 (2012).
    • (2012) PLoS Pathog. , vol.8 , pp. e1002859
    • Reguera, J.1
  • 31
    • 0032509096 scopus 로고    scopus 로고
    • Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues
    • Eckert, D. M., Malashkevich, V. N. & Kim, P. S. Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues. J. Mol. Biol. 284, 859-865 (1998).
    • (1998) J. Mol. Biol. , vol.284 , pp. 859-865
    • Eckert, D.M.1    Malashkevich, V.N.2    Kim, P.S.3
  • 32
    • 48249140239 scopus 로고    scopus 로고
    • Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution
    • Zeng, Q., Langereis, M. A., van Vliet, A. L., Huizinga, E. G. & de Groot, R. J. Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution. Proc. Natl Acad. Sci. USA 105, 9065-9069 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 9065-9069
    • Zeng, Q.1    Langereis, M.A.2    Van Vliet, A.L.3    Huizinga, E.G.4    De Groot, R.J.5
  • 33
    • 79952438103 scopus 로고    scopus 로고
    • Precise beam-tilt alignment and collimation are required to minimize the phase error associated with coma in high-resolution cryo-EM
    • Glaeser, R. M., Typke, D., Tiemeijer, P. C., Pulokas, J. & Cheng, A. Precise beam-tilt alignment and collimation are required to minimize the phase error associated with coma in high-resolution cryo-EM. J. Struct. Biol. 174, 1-10 (2011).
    • (2011) J. Struct. Biol. , vol.174 , pp. 1-10
    • Glaeser, R.M.1    Typke, D.2    Tiemeijer, P.C.3    Pulokas, J.4    Cheng, A.5
  • 34
    • 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
  • 35
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nature Methods 10, 584-590 (2013).
    • (2013) Nature Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 36
    • 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
  • 37
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J. A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 38
    • 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
  • 39
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 40
    • 84888059421 scopus 로고    scopus 로고
    • Optimod-an automated approach for constructing and optimizing initial models for single-particle electron microscopy
    • Lyumkis, D., Vinterbo, S., Potter, C. S. & Carragher, B. Optimod-an automated approach for constructing and optimizing initial models for single-particle electron microscopy. J. Struct. Biol. 184, 417-426 (2013).
    • (2013) J. Struct. Biol. , vol.184 , pp. 417-426
    • Lyumkis, D.1    Vinterbo, S.2    Potter, C.S.3    Carragher, B.4
  • 41
    • 84878580683 scopus 로고    scopus 로고
    • Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles
    • Bai, X. C., Fernandez, I. S., McMullan, G. & Scheres, S. H. Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles. eLife 2, e00461 (2013).
    • (2013) ELife , vol.2 , pp. e00461
    • Bai, X.C.1    Fernandez, I.S.2    McMullan, G.3    Scheres, S.H.4
  • 42
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megadalton cryo-EM particles
    • Scheres, S. H. Beam-induced motion correction for sub-megadalton cryo-EM particles. eLife 3, e03665 (2014).
    • (2014) ELife , vol.3 , pp. e03665
    • Scheres, S.H.1
  • 43
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres, S. H. & Chen, S. Prevention of overfitting in cryo-EM structure determination. Nature Methods 9, 853-854 (2012).
    • (2012) Nature Methods , vol.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 44
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • Chen, S. et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135, 24-35 (2013).
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1
  • 45
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • Goddard, T. D., Huang, C. C. & Ferrin, T. E. Visualizing density maps with UCSF Chimera. J. Struct. Biol. 157, 281-287 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 47
    • 84885431817 scopus 로고    scopus 로고
    • High-resolution comparative modeling with RosettaCM
    • Song, Y. et al. High-resolution comparative modeling with RosettaCM. Structure 21, 1735-1742 (2013).
    • (2013) Structure , vol.21 , pp. 1735-1742
    • Song, Y.1
  • 48
    • 84881282403 scopus 로고    scopus 로고
    • Cryo-EM model validation using independent map reconstructions
    • DiMaio, F., Zhang, J., Chiu, W. & Baker, D. Cryo-EM model validation using independent map reconstructions. Protein Sci. 22, 865-868 (2013).
    • (2013) Protein Sci. , vol.22 , pp. 865-868
    • DiMaio, F.1    Zhang, J.2    Chiu, W.3    Baker, D.4
  • 49
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 50
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 51
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L. & Rosenstrom, P. Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549 (2010).
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenstrom, P.2
  • 52
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16, 10881-10890 (1988).
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 53
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • Robert, X. & Gouet, P. Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res. 42, W320-W324 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.