Structures of human antibodies bound to SARS-CoV-2 spike reveal common epitopes and recurrent features of antibodies
暂无分享,去创建一个
M. Nussenzweig | P. Bieniasz | A. West | A. Hurley | P. Bjorkman | D. Robbiani | N. G. Sharaf | Y. Weisblum | T. Hatziioannou | C. Gaebler | C. Barnes | Kathryn E Huey-Tubman | Magnus A. G. Hoffmann | Pauline R Hoffman | Nicholas Koranda | H. Gristick | F. Muecksch | Shlomo Finkin | K. Millard | F. Schmidt | M. Caskey | J. C. Cetrulo Lorenzi | Thomas Hagglof | Katrina G. Millard | Pauline R. Hoffman | A. West
[1] V. Giudicelli,et al. IMGT(R), the international ImMunoGeneTics information system(R). , 2022 .
[2] D. Burton,et al. Isolation of potent SARS-CoV-2 neutralizing antibodies and protection from disease in a small animal model , 2020, Science.
[3] C. Rice,et al. Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals , 2020, Nature.
[4] Linqi Zhang,et al. Human neutralizing antibodies elicited by SARS-CoV-2 infection , 2020, Nature.
[5] Amalio Telenti,et al. Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody , 2020, Nature.
[6] X. Xie,et al. Potent Neutralizing Antibodies against SARS-CoV-2 Identified by High-Throughput Single-Cell Sequencing of Convalescent Patients’ B Cells , 2020, Cell.
[7] C. Rice,et al. Convergent Antibody Responses to SARS-CoV-2 Infection in Convalescent Individuals , 2020, bioRxiv.
[8] F. Grosveld,et al. Publisher Correction: A human monoclonal antibody blocking SARS-CoV-2 infection , 2020, Nature Communications.
[9] Samuel B. Day,et al. Rapid isolation and profiling of a diverse panel of human monoclonal antibodies targeting the SARS-CoV-2 spike protein , 2020, bioRxiv.
[10] L. Stamatatos,et al. Characterization of neutralizing antibodies from a SARS-CoV-2 infected individual , 2020, bioRxiv.
[11] M. V. van Breemen,et al. Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability , 2020, Science.
[12] D. Burton,et al. Rapid isolation of potent SARS-CoV-2 neutralizing antibodies and protection in a small animal model , 2020, bioRxiv.
[13] A. Sette,et al. The RBD Of The Spike Protein Of SARS-Group Coronaviruses Is A Highly Specific Target Of SARS-CoV-2 Antibodies But Not Other Pathogenic Human and Animal Coronavirus Antibodies , 2020, medRxiv.
[14] Qiang Zhou,et al. A potent neutralizing human antibody reveals the N-terminal domain of the Spike protein of SARS-CoV-2 as a site of vulnerability , 2020, bioRxiv.
[15] F. Gao,et al. A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2 , 2020, Science.
[16] D. Montefiori,et al. Spike mutation pipeline reveals the emergence of a more transmissible form of SARS-CoV-2 , 2020, bioRxiv.
[17] J. Bloom,et al. Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays , 2020, bioRxiv.
[18] Wenhui Li,et al. The SARS-CoV-2 receptor-binding domain elicits a potent neutralizing response without antibody-dependent enhancement , 2020, bioRxiv.
[19] J. Zhao,et al. Human monoclonal antibodies block the binding of SARS-CoV-2 spike protein to angiotensin converting enzyme 2 receptor , 2020, Cellular & Molecular Immunology.
[20] Amalio Telenti,et al. Structural and functional analysis of a potent sarbecovirus neutralizing antibody , 2020, bioRxiv.
[21] Baoying Huang,et al. Robust neutralization assay based on SARS-CoV-2 S-bearing vesicular stomatitis virus (VSV) pseudovirus and ACE2-overexpressed BHK21 cells , 2020, bioRxiv.
[22] Y. Wen,et al. Neutralizing antibody responses to SARS-CoV-2 in a COVID-19 recovered patient cohort and their implications , 2020, medRxiv.
[23] I. Wilson,et al. A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV , 2020, Science.
[24] Yan Liu,et al. Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV , 2020, Nature Communications.
[25] Lei Liu,et al. Potent human neutralizing antibodies elicited by SARS-CoV-2 infection , 2020, bioRxiv.
[26] K. Shi,et al. Structural basis of receptor recognition by SARS-CoV-2 , 2020, Nature.
[27] Qi Zhao,et al. Perspectives on therapeutic neutralizing antibodies against the Novel Coronavirus SARS-CoV-2 , 2020, International journal of biological sciences.
[28] Nicholas C. Wu,et al. A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV , 2020, Science.
[29] Frank Grosveld,et al. A human monoclonal antibody blocking SARS-CoV-2 infection , 2020, Nature Communications.
[30] A. Walls,et al. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein , 2020, Cell.
[31] G. Herrler,et al. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor , 2020, Cell.
[32] Qiang Zhou,et al. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2 , 2020, Science.
[33] Young-Jun Park,et al. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein , 2020, Cell.
[34] B. Graham,et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation , 2020, Science.
[35] A. Ward,et al. Structure and immune recognition of the porcine epidemic diarrhea virus spike protein , 2020, bioRxiv.
[36] E. Holmes,et al. A new coronavirus associated with human respiratory disease in China , 2020, Nature.
[37] Kai Zhao,et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin , 2020, Nature.
[38] Ralph S. Baric,et al. Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus , 2020, Journal of Virology.
[39] J. Nie,et al. Establishment and validation of a pseudovirus neutralization assay for SARS-CoV-2 , 2020, Emerging microbes & infections.
[40] D. Burton,et al. Mapping polyclonal antibody responses in non-human primates vaccinated with HIV Env trimer subunit vaccines , 2019, bioRxiv.
[41] John L Rubinstein,et al. The human coronavirus HCoV-229E S-protein structure and receptor binding , 2019, eLife.
[42] J. McLellan,et al. The 3.1-Angstrom Cryo-electron Microscopy Structure of the Porcine Epidemic Diarrhea Virus Spike Protein in the Prefusion Conformation , 2019, Journal of Virology.
[43] T. Fung,et al. Human Coronavirus: Host-Pathogen Interaction. , 2019, Annual review of microbiology.
[44] D. Veesler,et al. Structural insights into coronavirus entry , 2019, Advances in Virus Research.
[45] A. Walls,et al. Structural basis for human coronavirus attachment to sialic acid receptors , 2019, Nature Structural & Molecular Biology.
[46] J. Mascola,et al. Broad and Potent Neutralizing Antibodies Recognize the Silent Face of the HIV Envelope , 2019, Immunity.
[47] A. Walls,et al. Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion , 2019, Cell.
[48] F. Grosveld,et al. Towards a solution to MERS: protective human monoclonal antibodies targeting different domains and functions of the MERS-coronavirus spike glycoprotein , 2019, Emerging microbes & infections.
[49] D. Burton,et al. Commonality despite exceptional diversity in the baseline human antibody repertoire , 2018, Nature.
[50] P. Adams,et al. A fully automatic method yielding initial models from high-resolution cryo-electron microscopy maps , 2018, Nature Methods.
[51] Daniel Wrapp,et al. Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis , 2018, Scientific Reports.
[52] D. Burton,et al. Electron-Microscopy-Based Epitope Mapping Defines Specificities of Polyclonal Antibodies Elicited during HIV-1 BG505 Envelope Trimer Immunization , 2018, Immunity.
[53] Thomas C Terwilliger,et al. A fully automatic method yielding initial models from high-resolution electron cryo-microscopy maps , 2018, Nature Methods.
[54] Trevor Bedford,et al. Nextstrain: real-time tracking of pathogen evolution , 2017, bioRxiv.
[55] A. Walls,et al. Glycan Shield and Fusion Activation of a Deltacoronavirus Spike Glycoprotein Fine-Tuned for Enteric Infections , 2017, Journal of Virology.
[56] Fang Li,et al. Cryo-Electron Microscopy Structure of Porcine Deltacoronavirus Spike Protein in the Prefusion State , 2017, Journal of Virology.
[57] A. Walls,et al. Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion , 2017, Proceedings of the National Academy of Sciences.
[58] Barney S. Graham,et al. Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen , 2017, Proceedings of the National Academy of Sciences.
[59] Yi Shi,et al. Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains , 2017, Nature Communications.
[60] Yuelong Shu,et al. GISAID: Global initiative on sharing all influenza data – from vision to reality , 2017, Euro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin.
[61] David J. Fleet,et al. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination , 2017, Nature Methods.
[62] Stefan Elbe,et al. Data, disease and diplomacy: GISAID's innovative contribution to global health , 2017, Global challenges.
[63] Haixia Zhou,et al. Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding , 2016, Cell Research.
[64] C. Rice,et al. Supplemental Information Identification of Interferon-stimulated Genes with Antiretroviral Activity , 2022 .
[65] M. Nussenzweig,et al. Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site , 2016, Nature Structural &Molecular Biology.
[66] D. Falzarano,et al. SARS and MERS: recent insights into emerging coronaviruses , 2016, Nature Reviews Microbiology.
[67] Muyuan Chen,et al. High resolution single particle refinement in EMAN2.1. , 2016, Methods.
[68] Barney S. Graham,et al. Pre-fusion structure of a human coronavirus spike protein , 2016, Nature.
[69] F. Dimaio,et al. Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer , 2016, Nature.
[70] N. Grigorieff,et al. CTFFIND4: Fast and accurate defocus estimation from electron micrographs , 2015, bioRxiv.
[71] A. McDowall,et al. Broadly Neutralizing Antibody 8ANC195 Recognizes Closed and Open States of HIV-1 Env , 2015, Cell.
[72] Ulas Bagci,et al. Evaluation of candidate vaccine approaches for MERS-CoV , 2015, Nature Communications.
[73] Lisa E. Gralinski,et al. Molecular pathology of emerging coronavirus infections , 2014, The Journal of pathology.
[74] Patrice Duroux,et al. IMGT®, the international ImMunoGeneTics information system® 25 years on , 2014, Nucleic Acids Res..
[75] Jiye Shi,et al. SAbDab: the structural antibody database , 2013, Nucleic Acids Res..
[76] Ralph S. Baric,et al. A decade after SARS: strategies for controlling emerging coronaviruses , 2013, Nature Reviews Microbiology.
[77] Christian Drosten,et al. Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC , 2013, Nature.
[78] K. Katoh,et al. MAFFT Multiple Sequence Alignment Software Version 7: Improvements in Performance and Usability , 2013, Molecular biology and evolution.
[79] L. Enjuanes,et al. Structural Bases of Coronavirus Attachment to Host Aminopeptidase N and Its Inhibition by Neutralizing Antibodies , 2012, PLoS pathogens.
[80] D. Higgins,et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega , 2011, Molecular systems biology.
[81] Randy J. Read,et al. Overview of the CCP4 suite and current developments , 2011, Acta crystallographica. Section D, Biological crystallography.
[82] I. Wilson,et al. A structural analysis of M protein in coronavirus assembly and morphology , 2010, Journal of Structural Biology.
[83] S. Plotkin. Correlates of Protection Induced by Vaccination , 2010, Clinical and Vaccine Immunology.
[84] Pamela J. Bjorkman,et al. Few and Far Between: How HIV May Be Evading Antibody Avidity , 2010, PLoS pathogens.
[85] O. Gascuel,et al. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. , 2010, Systematic biology.
[86] P. Emsley,et al. Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.
[87] Paramvir S. Dehal,et al. FastTree 2 – Approximately Maximum-Likelihood Trees for Large Alignments , 2010, PloS one.
[88] Randy J. Read,et al. Acta Crystallographica Section D Biological , 2003 .
[89] Vincent B. Chen,et al. Correspondence e-mail: , 2000 .
[90] S. Plotkin,et al. Vaccines: correlates of vaccine-induced immunity. , 2008, Clinical infectious diseases : an official publication of the Infectious Diseases Society of America.
[91] R. Baric,et al. Structural Basis for Potent Cross-Neutralizing Human Monoclonal Antibody Protection against Lethal Human and Zoonotic Severe Acute Respiratory Syndrome Coronavirus Challenge , 2008, Journal of Virology.
[92] Randy J. Read,et al. Phaser crystallographic software , 2007, Journal of applied crystallography.
[93] Conrad C. Huang,et al. Visualizing density maps with UCSF Chimera. , 2007, Journal of structural biology.
[94] William C. Hwang,et al. Structural Basis of Neutralization by a Human Anti-severe Acute Respiratory Syndrome Spike Protein Antibody, 80R* , 2006, Journal of Biological Chemistry.
[95] Yang Feng,et al. Structure of Severe Acute Respiratory Syndrome Coronavirus Receptor-binding Domain Complexed with Neutralizing Antibody* , 2006, Journal of Biological Chemistry.
[96] David N Mastronarde,et al. Automated electron microscope tomography using robust prediction of specimen movements. , 2005, Journal of structural biology.
[97] Ying Tang,et al. Ultra-potent antibodies against respiratory syncytial virus: effects of binding kinetics and binding valence on viral neutralization. , 2005, Journal of molecular biology.
[98] Itay Mayrose,et al. ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures , 2005, Nucleic Acids Res..
[99] Conrad C. Huang,et al. UCSF Chimera—A visualization system for exploratory research and analysis , 2004, J. Comput. Chem..
[100] S. Plotkin. Immunologic correlates of protection induced by vaccination , 2001, The Pediatric infectious disease journal.