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Volumn 547, Issue 7663, 2017, Pages 360-361

Open and closed structures reveal allostery and pliability in the HIV-1 envelope spike

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; CD4 ANTIGEN; CCR5 PROTEIN, HUMAN; CHEMOKINE RECEPTOR CCR5; GLYCOPROTEIN GP 41; IMMUNOGLOBULIN F(AB) FRAGMENT; LIGAND; VIRUS ENVELOPE PROTEIN; VIRUS RECEPTOR;

EID: 85025476641     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature23010     Document Type: Article
Times cited : (200)

References (53)
  • 3
    • 84961231130 scopus 로고    scopus 로고
    • Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
    • Lee, J. H., Ozorowski, G. & Ward, A. B. Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer. Science 351, 1043-1048 (2016).
    • (2016) Science , vol.351 , pp. 1043-1048
    • Lee, J.H.1    Ozorowski, G.2    Ward, A.B.3
  • 4
    • 84884678235 scopus 로고    scopus 로고
    • A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies
    • Sanders, R. W. et al. A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies. PLoS Pathog. 9, e1003618 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003618
    • Sanders, R.W.1
  • 5
    • 84969835812 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies to HIV and their role in vaccine design
    • Burton, D. R. & Hangartner, L. Broadly neutralizing antibodies to HIV and their role in vaccine design. Annu. Rev. Immunol. 34, 635-659 (2016).
    • (2016) Annu. Rev. Immunol. , vol.34 , pp. 635-659
    • Burton, D.R.1    Hangartner, L.2
  • 6
    • 84929896699 scopus 로고    scopus 로고
    • Antibody responses to envelope glycoproteins in HIV-1 infection
    • Burton, D. R. & Mascola, J. R. Antibody responses to envelope glycoproteins in HIV-1 infection. Nat. Immunol. 16, 571-576 (2015).
    • (2015) Nat. Immunol. , vol.16 , pp. 571-576
    • Burton, D.R.1    Mascola, J.R.2
  • 7
    • 84883796903 scopus 로고    scopus 로고
    • Antibodies in HIV-1 vaccine development and therapy
    • Klein, F. et al. Antibodies in HIV-1 vaccine development and therapy. Science 341, 1199-1204 (2013).
    • (2013) Science , vol.341 , pp. 1199-1204
    • Klein, F.1
  • 8
    • 84894173514 scopus 로고    scopus 로고
    • Structural insights on the role of antibodies in HIV-1 vaccine and therapy
    • West, A. P., Jr et al. Structural insights on the role of antibodies in HIV-1 vaccine and therapy. Cell 156, 633-648 (2014).
    • (2014) Cell , vol.156 , pp. 633-648
    • West, A.P.1
  • 10
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric HIV-1 envelope glycoprotein activation
    • Tran, E. E. H. et al. Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog. 8, e1002797 (2012).
    • (2012) PLoS Pathog. , vol.8 , pp. e1002797
    • Tran, E.E.H.1
  • 11
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P. D. et al. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648-659 (1998).
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1
  • 12
    • 84904127504 scopus 로고    scopus 로고
    • CD4-induced activation in a soluble HIV-1 Env trimer
    • Guttman, M. et al. CD4-induced activation in a soluble HIV-1 Env trimer. Structure 22, 974-984 (2014).
    • (2014) Structure , vol.22 , pp. 974-984
    • Guttman, M.1
  • 13
    • 84909606387 scopus 로고    scopus 로고
    • Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
    • Munro, J. B. et al. Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions. Science 346, 759-763 (2014).
    • (2014) Science , vol.346 , pp. 759-763
    • Munro, J.B.1
  • 14
    • 84923172318 scopus 로고    scopus 로고
    • A native-like SOSIP.664 trimer based on an HIV-1 subtype B env gene
    • Pugach, P. et al. A native-like SOSIP.664 trimer based on an HIV-1 subtype B env gene. J. Virol. 89, 3380-3395 (2015).
    • (2015) J. Virol. , vol.89 , pp. 3380-3395
    • Pugach, P.1
  • 15
    • 84937469192 scopus 로고    scopus 로고
    • HIV-1 vaccines. HIV-1 neutralizing antibodies induced by native-like envelope trimers
    • Sanders, R. W. et al. HIV-1 vaccines. HIV-1 neutralizing antibodies induced by native-like envelope trimers. Science 349, aac4223 (2015).
    • (2015) Science , vol.349 , pp. aac4223
    • Sanders, R.W.1
  • 16
    • 84887307095 scopus 로고    scopus 로고
    • Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation
    • Ringe, R. P. et al. Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation. Proc. Natl Acad. Sci. USA 110, 18256-18261 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 18256-18261
    • Ringe, R.P.1
  • 17
    • 84936846696 scopus 로고    scopus 로고
    • Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env
    • Kwon, Y. D. et al. Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env. Nat. Struct. Mol. Biol. 22, 522-531 (2015).
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , pp. 522-531
    • Kwon, Y.D.1
  • 18
    • 77749329921 scopus 로고    scopus 로고
    • Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions
    • Finzi, A. et al. Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions. Mol. Cell 37, 656-667 (2010).
    • (2010) Mol. Cell , vol.37 , pp. 656-667
    • Finzi, A.1
  • 19
    • 0034255034 scopus 로고    scopus 로고
    • Energetics of the HIV gp120-CD4 binding reaction
    • Myszka, D. G. et al. Energetics of the HIV gp120-CD4 binding reaction. Proc. Natl Acad. Sci. USA 97, 9026-9031 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9026-9031
    • Myszka, D.G.1
  • 20
    • 75749133275 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility
    • Pancera, M. et al. Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc. Natl Acad. Sci. USA 107, 1166-1171 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1166-1171
    • Pancera, M.1
  • 21
    • 85013157801 scopus 로고    scopus 로고
    • Quaternary contact in the initial interaction of CD4 with the HIV-1 envelope trimer
    • Liu, Q. et al. Quaternary contact in the initial interaction of CD4 with the HIV-1 envelope trimer. Nat. Struct. Mol. Biol. 24, 370-378 (2017).
    • (2017) Nat. Struct. Mol. Biol. , vol.24 , pp. 370-378
    • Liu, Q.1
  • 22
    • 84882589754 scopus 로고    scopus 로고
    • Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies
    • Zhou, T. et al. Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies. Immunity 39, 245-258 (2013).
    • (2013) Immunity , vol.39 , pp. 245-258
    • Zhou, T.1
  • 23
    • 33847101745 scopus 로고    scopus 로고
    • Structural definition of a conserved neutralization epitope on HIV-1 gp120
    • Zhou, T. et al. Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 445, 732-737 (2007).
    • (2007) Nature , vol.445 , pp. 732-737
    • Zhou, T.1
  • 24
    • 57749083487 scopus 로고    scopus 로고
    • Role of the HIV gp120 conserved domain 1 in processing and viral entry
    • Wang, J., Sen, J., Rong, L. & Caffrey, M. Role of the HIV gp120 conserved domain 1 in processing and viral entry. J. Biol. Chem. 283, 32644-32649 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 32644-32649
    • Wang, J.1    Sen, J.2    Rong, L.3    Caffrey, M.4
  • 25
    • 79953086675 scopus 로고    scopus 로고
    • Resistance of a human immunodeficiency virus type 1 isolate to a small molecule CCR5 inhibitor can involve sequence changes in both gp120 and gp41
    • Anastassopoulou, C. G. et al. Resistance of a human immunodeficiency virus type 1 isolate to a small molecule CCR5 inhibitor can involve sequence changes in both gp120 and gp41. Virology 413, 47-59 (2011).
    • (2011) Virology , vol.413 , pp. 47-59
    • Anastassopoulou, C.G.1
  • 26
    • 65249151382 scopus 로고    scopus 로고
    • Resistance to CCR5 inhibitors caused by sequence changes in the fusion peptide of HIV-1 gp41
    • Anastassopoulou, C. G., Ketas, T. J., Klasse, P. J. & Moore, J. P. Resistance to CCR5 inhibitors caused by sequence changes in the fusion peptide of HIV-1 gp41. Proc. Natl Acad. Sci. USA 106, 5318-5323 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 5318-5323
    • Anastassopoulou, C.G.1    Ketas, T.J.2    Klasse, P.J.3    Moore, J.P.4
  • 27
    • 84884673669 scopus 로고    scopus 로고
    • Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex
    • Tan, Q. et al. Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex. Science 341, 1387-1390 (2013).
    • (2013) Science , vol.341 , pp. 1387-1390
    • Tan, Q.1
  • 28
    • 0034517231 scopus 로고    scopus 로고
    • Leginon: An automated system for acquisition of images from vitreous ice specimens
    • Carragher, B. et al. Leginon: an automated system for acquisition of images from vitreous ice specimens. J. Struct. Biol. 132, 33-45 (2000).
    • (2000) J. Struct. Biol. , vol.132 , pp. 33-45
    • Carragher, B.1
  • 29
    • 0033166275 scopus 로고    scopus 로고
    • Leginon: A system for fully automated acquisition of 1000 electron micrographs a day
    • Potter, C. S. et al. Leginon: a system for fully automated acquisition of 1000 electron micrographs a day. Ultramicroscopy 77, 153-161 (1999).
    • (1999) Ultramicroscopy , vol.77 , pp. 153-161
    • Potter, C.S.1
  • 30
    • 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
  • 31
    • 85014129582 scopus 로고    scopus 로고
    • MotionCor2: Anisotropic correction of beam-induced motion for improved cryo-electron microscopy
    • Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331-332 (2017).
    • (2017) Nat. Methods , vol.14 , pp. 331-332
    • Zheng, S.Q.1
  • 32
    • 84955216953 scopus 로고    scopus 로고
    • Gctf: Real-time CTF determination and correction
    • Zhang, K. Gctf: real-time CTF determination and correction. J. Struct. Biol. 193, 1-12 (2016).
    • (2016) J. Struct. Biol. , vol.193 , pp. 1-12
    • Zhang, K.1
  • 33
    • 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
  • 34
    • 0142059303 scopus 로고    scopus 로고
    • Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking
    • Ogura, T., Iwasaki, K. & Sato, C. Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking. J. Struct. Biol. 143, 185-200 (2003).
    • (2003) J. Struct. Biol. , vol.143 , pp. 185-200
    • Ogura, T.1    Iwasaki, K.2    Sato, C.3
  • 36
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. W. 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.W.1
  • 37
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis, D. et al. Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 342, 1484-1490 (2013).
    • (2013) Science , vol.342 , pp. 1484-1490
    • Lyumkis, D.1
  • 38
    • 84883447961 scopus 로고    scopus 로고
    • Likelihood-based classification of cryo-EM images using FREALIGN
    • Lyumkis, D., Brilot, A. F., Theobald, D. L. & Grigorieff, N. Likelihood-based classification of cryo-EM images using FREALIGN. J. Struct. Biol. 183, 377-388 (2013).
    • (2013) J. Struct. Biol. , vol.183 , pp. 377-388
    • Lyumkis, D.1    Brilot, A.F.2    Theobald, D.L.3    Grigorieff, N.4
  • 39
    • 84855818650 scopus 로고    scopus 로고
    • A Bayesian view on cryo-EM structure determination
    • Scheres, S. H. W. A Bayesian view on cryo-EM structure determination. J. Mol. Biol. 415, 406-418 (2012).
    • (2012) J. Mol. Biol. , vol.415 , pp. 406-418
    • Scheres, S.H.W.1
  • 40
    • 33845939047 scopus 로고    scopus 로고
    • Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization
    • Scheres, S. H. W. et al. Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization. Nat. Methods 4, 27-29 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 27-29
    • Scheres, S.H.W.1
  • 41
    • 84960173062 scopus 로고    scopus 로고
    • Pre-fusion structure of a human coronavirus spike protein
    • Kirchdoerfer, R. N. et al. Pre-fusion structure of a human coronavirus spike protein. Nature 531, 118-121 (2016).
    • (2016) Nature , vol.531 , pp. 118-121
    • Kirchdoerfer, R.N.1
  • 43
    • 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. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 44
    • 84926520440 scopus 로고    scopus 로고
    • Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement
    • DiMaio, F. et al. Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement. Nat. Methods 12, 361-365 (2015).
    • (2015) Nat. Methods , vol.12 , pp. 361-365
    • DiMaio, F.1
  • 45
    • 68949187842 scopus 로고    scopus 로고
    • Refinement of protein structures into low-resolution density maps using rosetta
    • DiMaio, F., Tyka, M. D., Baker, M. L., Chiu, W. & Baker, D. Refinement of protein structures into low-resolution density maps using rosetta. J. Mol. Biol. 392, 181-190 (2009).
    • (2009) J. Mol. Biol. , vol.392 , pp. 181-190
    • DiMaio, F.1    Tyka, M.D.2    Baker, M.L.3    Chiu, W.4    Baker, D.5
  • 47
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 48
    • 13244253766 scopus 로고    scopus 로고
    • Pdb-care (PDB carbohydrate residue check): A program to support annotation of complex carbohydrate structures in PDB files
    • Lütteke, T. & von der Lieth, C.-W. pdb-care (PDB carbohydrate residue check): a program to support annotation of complex carbohydrate structures in PDB files. BMC Bioinformatics 5, 69 (2004).
    • (2004) BMC Bioinformatics , vol.5 , pp. 69
    • Lütteke, T.1    Von Der-Lieth, C.-W.2
  • 49
    • 13444283836 scopus 로고    scopus 로고
    • Carbohydrate structure suite (CSS): Analysis of carbohydrate 3D structures derived from the PDB
    • Lütteke, T., Frank, M. & von der Lieth, C.-W. Carbohydrate Structure Suite (CSS): analysis of carbohydrate 3D structures derived from the PDB. Nucleic Acids Res. 33, D242-D246 (2005).
    • (2005) Nucleic Acids Res. , vol.33 , pp. D242-D246
    • Lütteke, T.1    Frank, M.2    Von Der-Lieth, C.-W.3
  • 50
    • 84959080555 scopus 로고    scopus 로고
    • EMRinger: Side chain-directed model and map validation for 3D cryo-electron microscopy
    • Barad, B. A. et al. EMRinger: side chain-directed model and map validation for 3D cryo-electron microscopy. Nat. Methods 12, 943-946 (2015).
    • (2015) Nat. Methods , vol.12 , pp. 943-946
    • Barad, B.A.1
  • 51
    • 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
  • 53
    • 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


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