Longitudinal Isolation of Potent Near-Germline SARS-CoV-2-Neutralizing Antibodies from COVID-19 Patients
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L. Gieselmann | N. Pfeifer | C. Wendtner | S. Becker | R. Diskin | V. Krähling | P. Schommers | M. Vehreschild | H. Cohen-Dvashi | M. Koch | H. Janicki | S. Halwe | A. Kupke | R. Brinker | Simone Lederer | F. Klein | H. Gruell | M. Korenkov | Christoph Kreer | T. Wolf | K. Vanshylla | Matthias Zehner | V. Di Cristanziano | M. Ercanoglu | Timm Weber | Artem Ashurov | Cornelius Rohde | Sandro Halwe | Verena Krähling
[1] L. Gieselmann,et al. Longitudinal Isolation of Potent Near-Germline SARS-CoV-2-Neutralizing Antibodies from COVID-19 Patients , 2020, Cell.
[2] X. Tang,et al. Clinical and immunological assessment of asymptomatic SARS-CoV-2 infections , 2020, Nature Medicine.
[3] J. Sodroski,et al. Potent Neutralizing Antibodies Directed to Multiple Epitopes on SARS-CoV-2 Spike , 2020, bioRxiv.
[4] R. Welsh,et al. Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail , 2020, Science.
[5] G. Atwal,et al. Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies , 2020, Science.
[6] D. Burton,et al. Isolation of potent SARS-CoV-2 neutralizing antibodies and protection from disease in a small animal model , 2020, Science.
[7] J. Dye,et al. Broad neutralization of SARS-related viruses by human monoclonal antibodies , 2020, Science.
[8] C. Rice,et al. Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals , 2020, Nature.
[9] L. Stamatatos,et al. Analysis of a SARS-CoV-2-Infected Individual Reveals Development of Potent Neutralizing Antibodies with Limited Somatic Mutation , 2020, Immunity.
[10] B. Haynes,et al. Pandemic Preparedness: Developing Vaccines and Therapeutic Antibodies For COVID-19 , 2020, Cell.
[11] William J. Liu,et al. A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2 , 2020, Nature.
[12] Linqi Zhang,et al. Human neutralizing antibodies elicited by SARS-CoV-2 infection , 2020, Nature.
[13] Lisa E. Gralinski,et al. Potently neutralizing human antibodies that block SARS-CoV-2 receptor binding and protect animals , 2020, bioRxiv.
[14] J. Greenbaum,et al. Targets of T Cell Responses to SARS-CoV-2 Coronavirus in Humans with COVID-19 Disease and Unexposed Individuals , 2020, Cell.
[15] Yanhu Li,et al. Isolation of and Characterization of Neutralizing Antibodies to Covid-19 from a Large Human Naïve scFv Phage Display Library , 2020, bioRxiv.
[16] 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.
[17] Amalio Telenti,et al. Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody , 2020, Nature.
[18] Lisa E. Gralinski,et al. Potent neutralization of SARS-CoV-2 in vitro and in an animal model by a human monoclonal antibody , 2020, bioRxiv.
[19] Lisa E. Gralinski,et al. Rapid selection of a human monoclonal antibody that potently neutralizes SARS-CoV-2 in two animal models , 2020 .
[20] D. Burton,et al. Rational Vaccine Design in the Time of COVID-19 , 2020, Cell Host & Microbe.
[21] M. V. van Breemen,et al. Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability , 2020, Science.
[22] R. Rappuoli,et al. Identification of neutralizing human monoclonal antibodies from Italian Covid-19 convalescent patients , 2020, bioRxiv.
[23] F. Gao,et al. A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2 , 2020, Science.
[24] Hongbing Shen,et al. Neutralizing Antibodies Isolated by a site-directed Screening have Potent Protection on SARS-CoV-2 Infection , 2020, bioRxiv.
[25] Hongbing Shen,et al. Isolating multiple formats of human monoclonal neutralizing antibodies against SARS-CoV-2 by in vitro site-directed antibody screening , 2020 .
[26] Xinquan Wang,et al. Detection of SARS-CoV-2-Specific Humoral and Cellular Immunity in COVID-19 Convalescent Individuals , 2020, Immunity.
[27] X. Tang,et al. Antibody responses to SARS-CoV-2 in patients with COVID-19 , 2020, Nature Medicine.
[28] U. Reimer,et al. Presence of SARS-CoV-2 reactive T cells in COVID-19 patients and healthy donors , 2020, medRxiv.
[29] Jianhua Du,et al. Blocking antibodies against SARS-CoV-2 RBD isolated from a phage display antibody library using a competitive biopanning strategy , 2020, bioRxiv.
[30] M. Addo,et al. Safety and immunogenicity of a modified vaccinia virus Ankara vector vaccine candidate for Middle East respiratory syndrome: an open-label, phase 1 trial , 2020, The Lancet Infectious Diseases.
[31] Kaijun Jiang,et al. SARS‐CoV‐2 Seroconversion in Humans: A Detailed Protocol for a Serological Assay, Antigen Production, and Test Setup , 2020, Current protocols in microbiology.
[32] T. Jodlowski,et al. Pharmacologic Treatments for Coronavirus Disease 2019 (COVID-19): A Review. , 2020, JAMA.
[33] Yan Peng,et al. Effectiveness of convalescent plasma therapy in severe COVID-19 patients , 2020, Proceedings of the National Academy of Sciences.
[34] N. Callewaert,et al. Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies , 2020, Cell.
[35] Frank Grosveld,et al. A human monoclonal antibody blocking SARS-CoV-2 infection , 2020, Nature Communications.
[36] D. Watkins,et al. Longitudinal dynamics of the human B cell response to the yellow fever 17D vaccine , 2020, Proceedings of the National Academy of Sciences.
[37] A. Walls,et al. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein , 2020, Cell.
[38] 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.
[39] Young-Jun Park,et al. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein , 2020, Cell.
[40] B. Graham,et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation , 2020, Science.
[41] E. Dong,et al. An interactive web-based dashboard to track COVID-19 in real time , 2020, The Lancet Infectious Diseases.
[42] B. Graham,et al. Cryo-EM Structure of the 2019-nCoV Spike in the Prefusion Conformation , 2020, bioRxiv.
[43] Kai Zhao,et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin , 2020, Nature.
[44] Nico Pfeifer,et al. openPrimeR for multiplex amplification of highly diverse templates. , 2020, Journal of immunological methods.
[45] G. Gao,et al. A Novel Coronavirus from Patients with Pneumonia in China, 2019 , 2020, The New England journal of medicine.
[46] Y. Hu,et al. Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China , 2020, The Lancet.
[47] J. Bloom,et al. Restriction of HIV-1 Escape by a Highly Broad and Potent Neutralizing Antibody , 2020, Cell.
[48] T. Mora,et al. Exploiting B Cell Receptor Analyses to Inform on HIV-1 Vaccination Strategies , 2020, Vaccines.
[49] J. Sodroski,et al. SARS-CoV-2 neutralizing antibody responses are more robust in patients with severe disease , 2020, bioRxiv.
[50] Daniel Edler,et al. raxmlGUI 2.0 beta: a graphical interface and toolkit for phylogenetic analyses using RAxML , 2019, bioRxiv.
[51] M. Addo,et al. Polyclonal and convergent antibody response to Ebola virus vaccine rVSV-ZEBOV , 2019, Nature Medicine.
[52] Chaim A. Schramm,et al. Activation Dynamics and Immunoglobulin Evolution of Pre-existing and Newly Generated Human Memory B cell Responses to Influenza Hemagglutinin. , 2019, Immunity.
[53] A. Trkola,et al. Correlates of broadly neutralizing antibody development. , 2019, Current opinion in HIV and AIDS.
[54] S. Zolla-Pazner,et al. Vaccine-induced V1V2-specific antibodies control and or protect against infection with HIV, SIV and SHIV , 2019, Current opinion in HIV and AIDS.
[55] J. Sidney,et al. Longitudinal Analysis of the Human B Cell Response to Ebola Virus Infection , 2019, Cell.
[56] J. Dye,et al. Systematic Analysis of Monoclonal Antibodies against Ebola Virus GP Defines Features that Contribute to Protection , 2018, Cell.
[57] D. Burton,et al. Passive immunotherapy of viral infections: 'super-antibodies' enter the fray , 2018, Nature Reviews Immunology.
[58] Tongqing Zhou,et al. Identification of a CD4-Binding-Site Antibody to HIV that Evolved Near-Pan Neutralization Breadth. , 2016, Immunity.
[59] M. Nussenzweig,et al. Sequencing and cloning of antigen-specific antibodies from mouse memory B cells , 2016, Nature Protocols.
[60] Cinque S. Soto,et al. Vaccine-Induced Antibodies that Neutralize Group 1 and Group 2 Influenza A Viruses , 2016, Cell.
[61] P. Collins,et al. Structure and Function Analysis of an Antibody Recognizing All Influenza A Subtypes , 2016, Cell.
[62] Jian Yu,et al. Engineered Bispecific Antibodies with Exquisite HIV-1-Neutralizing Activity , 2016, Cell.
[63] James E. Crowe,et al. Cross-Reactive and Potent Neutralizing Antibody Responses in Human Survivors of Natural Ebolavirus Infection , 2016, Cell.
[64] A. Fauci,et al. Toward an HIV vaccine: A scientific journey , 2015, Science.
[65] R. Marschalek,et al. Optimized Sleeping Beauty transposons rapidly generate stable transgenic cell lines. , 2015, Biotechnology journal.
[66] David A. Hafler,et al. pRESTO: a toolkit for processing high-throughput sequencing raw reads of lymphocyte receptor repertoires , 2014, Bioinform..
[67] Alexandros Stamatakis,et al. RAxML version 8: a tool for phylogenetic analysis and post-analysis of large phylogenies , 2014, Bioinform..
[68] Florian Klein,et al. Antibodies in HIV-1 Vaccine Development and Therapy , 2013, Science.
[69] Philip R. Johnson,et al. Accelerating Next-Generation Vaccine Development for Global Disease Prevention , 2013, Science.
[70] Ning Ma,et al. IgBLAST: an immunoglobulin variable domain sequence analysis tool , 2013, Nucleic Acids Res..
[71] Michael Meyer-Hermann,et al. Germinal center B cells govern their own fate via antibody feedback , 2013, The Journal of experimental medicine.
[72] D. Higgins,et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega , 2011, Molecular systems biology.
[73] Ron Diskin,et al. Sequence and Structural Convergence of Broad and Potent HIV Antibodies That Mimic CD4 Binding , 2011, Science.
[74] J. Skehel,et al. A Neutralizing Antibody Selected from Plasma Cells That Binds to Group 1 and Group 2 Influenza A Hemagglutinins , 2011, Science.
[75] Mario Roederer,et al. Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1 , 2010, Science.
[76] David C Montefiori,et al. The role of antibodies in HIV vaccines. , 2010, Annual review of immunology.
[77] Andreas Radbruch,et al. Generation of stable monoclonal antibody-producing BCR+ human memory B cells by genetic programming , 2009, Nature Medicine.
[78] Pham Phung,et al. Broad and Potent Neutralizing Antibodies from an African Donor Reveal a New HIV-1 Vaccine Target , 2009, Science.
[79] D. Eisenberg,et al. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. , 1984, Journal of molecular biology.
[80] H. Kowarzyk. Structure and Function. , 1910, Nature.
[81] Captain Y. B. Nusfield,et al. Public Health , 1906, Canadian Medical Association journal.
[82] Feng-hua Liu,et al. A systematic analysis , 2020 .
[83] Michel C Nussenzweig,et al. Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning. , 2008, Journal of immunological methods.
[84] James R. Harris,et al. LONGITUDINAL DYNAMICS IN THE , 2005 .
[85] Hua,et al. Identification of , 2000, Journal of insect physiology.
[86] D. Sommers,et al. A longitudinal analysis , 1992 .
[87] F. Shlaeffer,et al. [Viral hemorrhagic fever]. , 1988, Harefuah.
[88] W. Mackenzie. Analysis of Memory , 1902, Nature.