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Longitudinal Isolation of Potent Near-Germline SARS-CoV-2-Neutralizing Antibodies from COVID-19 Patients

Kreer, Christoph, Zehner, Matthias, Weber, Timm, Ercanoglu, Meryem S., Gieselmann, Lutz, Rohde, Cornelius, Halwe, Sandro, Korenkov, Michael, Schommers, Philipp, Vanshylla, Kanika, Di Cristanziano, Veronica, Janicki, Hanna, Brinker, Reinhild, Ashurov, Artem, Krähling, Verena, Kupke, Alexandra, Cohen-Dvashi, Hadas, Koch, Manuel, Eckert, Jan Mathis, Lederer, Simone, Pfeifer, Nico, Wolf, Timo, Vehreschild, Maria J.G.T., Wendtner, Clemens, Diskin, Ron, Gruell, Henning, Becker, Stephan, Klein, Florian·2020·Cell
DOI 10.1016/j.cell.2020.06.044PMC PMC7355337

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  1. Andreano, 2020, Identification of neutralizing human monoclonal antibodies from Italian Covid-19 convalescent patients, bioRxiv
  2. Burton, 2020, Rational Vaccine Design in the Time of COVID-19, Cell Host Microbe, 27, 695, 10.1016/j.chom.2020.04.022 · DOI
  3. Cao, 2020, Potent neutralizing antibodies against SARS-CoV-2 identified by high-throughput single-cell sequencing of convalescent patients’ B cells, Cell., 10.1016/j.cell.2020.05.025 · DOI · Paper page
  4. Corti, 2011, A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins, Science, 333, 850, 10.1126/science.1205669 · DOI · Paper page
  5. Davis, 2019, Longitudinal Analysis of the Human B Cell Response to Ebola Virus Infection, Cell, 177, 1566, 10.1016/j.cell.2019.04.036 · DOI
  6. Dong, 2020, An interactive web-based dashboard to track COVID-19 in real time, Lancet Infect. Dis., 20, 533, 10.1016/S1473-3099(20)30120-1 · DOI · Paper page
  7. Duan, 2020, Effectiveness of convalescent plasma therapy in severe COVID-19 patients, Proc. Natl. Acad. Sci. USA, 117, 9490, 10.1073/pnas.2004168117 · DOI
  8. Edler, 2019, raxmlGUI 2.0 beta: a graphical interface and toolkit for phylogenetic analyses using RAxML, bioRxiv
  9. Ehrhardt, 2019, Polyclonal and convergent antibody response to Ebola virus vaccine rVSV-ZEBOV, Nat. Med., 25, 1589, 10.1038/s41591-019-0602-4 · DOI
  10. Eisenberg, 1984, Analysis of membrane and surface protein sequences with the hydrophobic moment plot, J. Mol. Biol., 179, 125, 10.1016/0022-2836(84)90309-7 · DOI
  11. Fauci, 2015, PUBLIC HEALTH. Toward an HIV vaccine: A scientific journey, Science, 349, 386, 10.1126/science.aac6300 · DOI
  12. Flyak, 2016, Cross-Reactive and Potent Neutralizing Antibody Responses in Human Survivors of Natural Ebolavirus Infection, Cell, 164, 392, 10.1016/j.cell.2015.12.022 · DOI
  13. Grifoni, 2020, Targets of T cell responses to SARS-CoV-2 coronavirus in humans with COVID-19 disease and unexposed individuals, Cell, 181, 1489, 10.1016/j.cell.2020.05.015 · DOI · Paper page
  14. Hoffmann, 2020, SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor, Cell, 181, 271, 10.1016/j.cell.2020.02.052 · DOI · Paper page
  15. Huang, 2016, Identification of a CD4-Binding-Site Antibody to HIV that Evolved Near-Pan Neutralization Breadth, Immunity, 45, 1108, 10.1016/j.immuni.2016.10.027 · DOI
  16. Huang, 2016, Engineered Bispecific Antibodies with Exquisite HIV-1-Neutralizing Activity, Cell, 165, 1621, 10.1016/j.cell.2016.05.024 · DOI
  17. Huang, 2020, Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China, Lancet, 395, 497, 10.1016/S0140-6736(20)30183-5 · DOI · Paper page
  18. Joyce, 2016, Vaccine-Induced Antibodies that Neutralize Group 1 and Group 2 Influenza A Viruses, Cell, 166, 609, 10.1016/j.cell.2016.06.043 · DOI · Paper page
  19. Kallewaard, 2016, Structure and Function Analysis of an Antibody Recognizing All Influenza A Subtypes, Cell, 166, 596, 10.1016/j.cell.2016.05.073 · DOI
  20. Klein, 2013, Antibodies in HIV-1 vaccine development and therapy, Science, 341, 1199, 10.1126/science.1241144 · DOI
  21. Koch, 2020, Safety and immunogenicity of a modified vaccinia virus Ankara vector vaccine candidate for Middle East respiratory syndrome: an open-label, phase 1 trial, The Lancet, 20, 827
  22. Koff, 2013, Accelerating next-generation vaccine development for global disease prevention, Science, 340, 1232910, 10.1126/science.1232910 · DOI · Paper page
  23. Kowarz, 2015, Optimized Sleeping Beauty transposons rapidly generate stable transgenic cell lines, Biotechnol. J., 10, 647, 10.1002/biot.201400821 · DOI
  24. Kreer, 2020, openPrimeR for multiplex amplification of highly diverse templates, J. Immunol. Methods, 480, 112752, 10.1016/j.jim.2020.112752 · DOI
  25. Kreer, 2020, Exploiting B Cell Receptor Analyses to Inform on HIV-1 Vaccination Strategies, Vaccines (Basel), 8, 13, 10.3390/vaccines8010013 · DOI
  26. Kwakkenbos, 2010, Generation of stable monoclonal antibody-producing B cell receptor-positive human memory B cells by genetic programming, Nat. Med., 16, 123, 10.1038/nm.2071 · DOI
  27. Li, 2020, Potent neutralization of SARS-CoV-2 in vitro and in an animal model by a human monoclonal antibody, bioRxiv
  28. Liu, 2020, Neutralizing Antibodies Isolated by a site-directed Screening have Potent Protection on SARS-CoV-2 Infection, bioRxiv
  29. Mascola, 2010, The role of antibodies in HIV vaccines, Annu. Rev. Immunol., 28, 413, 10.1146/annurev-immunol-030409-101256 · DOI
  30. Ni, 2020, Detection of SARS-CoV-2-Specific Humoral and Cellular Immunity in COVID-19 Convalescent Individuals, Immunity, 52, 971, 10.1016/j.immuni.2020.04.023 · DOI
  31. Pinto, 2020, Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody, Nature., 10.1038/s41586-020-2349-y · DOI · Paper page
  32. Rogers, 2020, Isolation of potent SARS-CoV-2 neutralizing antibodies and protection from disease in a small animal model, Science, 10.1126/science.abc7520 · DOI · Paper page
  33. Sanders, 2020, Pharmacologic Treatments for Coronavirus Disease 2019 (COVID-19): A Review, JAMA., 10.1001/jama.2020.6019 · DOI
  34. Saphire, 2018, Systematic Analysis of Monoclonal Antibodies against Ebola Virus GP Defines Features that Contribute to Protection, Cell, 174, 938, 10.1016/j.cell.2018.07.033 · DOI · Paper page
  35. Scheid, 2011, Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding, Science, 333, 1633, 10.1126/science.1207227 · DOI
  36. Schommers, 2020, Restriction of HIV-1 Escape by a Highly Broad and Potent Neutralizing Antibody, Cell, 180, 471, 10.1016/j.cell.2020.01.010 · DOI
  37. Sempowski, 2020, Pandemic Preparedness: Developing Vaccines and Therapeutic Antibodies For COVID-19, Cell, 181, 1458, 10.1016/j.cell.2020.05.041 · DOI
  38. Shi, 2020, A human neutralizing antibody targets the receptor binding site of SARS-CoV-2, Nature., 10.1038/s41586-020-2381-y · DOI · Paper page
  39. Sievers, 2011, Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega, Mol. Syst. Biol., 7, 539, 10.1038/msb.2011.75 · DOI
  40. Stadlbauer, 2020, SARS-CoV-2 Seroconversion in Humans: A Detailed Protocol for a Serological Assay, Antigen Production, and Test Setup, Curr. Protoc. Microbiol., 57, e100, 10.1002/cpmc.100 · DOI
  41. Stamatakis, 2014, RAxML version 8: a tool for phylogenetic analysis and post-analysis of large phylogenies, Bioinformatics, 30, 1312, 10.1093/bioinformatics/btu033 · DOI · Paper page
  42. Tiller, 2008, Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning, J. Immunol. Methods, 329, 112, 10.1016/j.jim.2007.09.017 · DOI
  43. Vander Heiden, 2014, pRESTO: a toolkit for processing high-throughput sequencing raw reads of lymphocyte receptor repertoires, Bioinformatics, 30, 1930, 10.1093/bioinformatics/btu138 · DOI
  44. von Boehmer, 2016, Sequencing and cloning of antigen-specific antibodies from mouse memory B cells, Nat. Protoc., 11, 1908, 10.1038/nprot.2016.102 · DOI
  45. Walker, 2018, Passive immunotherapy of viral infections: ‘super-antibodies’ enter the fray, Nat. Rev. Immunol., 18, 297, 10.1038/nri.2017.148 · DOI
  46. Walker, 2009, Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target, Science, 326, 285, 10.1126/science.1178746 · DOI
  47. Walls, 2020, Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein, Cell, 181, 281, 10.1016/j.cell.2020.02.058 · DOI · Paper page
  48. Wang, 2020, A human monoclonal antibody blocking SARS-CoV-2 infection, Nat. Commun., 11, 2251, 10.1038/s41467-020-16256-y · DOI
  49. Wec, 2020, Longitudinal dynamics of the human B cell response to the yellow fever 17D vaccine, Proc. Natl. Acad. Sci. USA, 117, 6675, 10.1073/pnas.1921388117 · DOI
  50. Wec, 2020, Broad neutralization of SARS-related viruses by human monoclonal antibodies, Science,, eabc7424
  51. Wrapp, 2020, Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies, Cell, 181, 1004, 10.1016/j.cell.2020.04.031 · DOI · Paper page
  52. Wu, 2010, Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1, Science, 329, 856, 10.1126/science.1187659 · DOI
  53. Wu, 2020, A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2, Science, 10.1126/science.abc2241 · DOI
  54. Ye, 2013, IgBLAST: an immunoglobulin variable domain sequence analysis tool, Nucleic Acids Res., 41, 10.1093/nar/gkt382 · DOI
  55. Yuan, 2020, Isolation of and Characterization of Neutralizing Antibodies to Covid-19 from a Large Human Naïve scFv Phage Display Library, bioRxiv
  56. Zeng, 2020, Blocking antibodies against SARS-CoV-2 RBD isolated from a phage display antibody library using a competitive biopanning strategy, bioRxiv
  57. Zhang, 2013, Germinal center B cells govern their own fate via antibody feedback, J. Exp. Med., 210, 457, 10.1084/jem.20120150 · DOI
  58. Zhou, 2020, A pneumonia outbreak associated with a new coronavirus of probable bat origin, Nature, 579, 270, 10.1038/s41586-020-2012-7 · DOI · Paper page
  59. Zolla-Pazner, 2019, Vaccine-induced V1V2-specific antibodies control and or protect against infection with HIV, SIV and SHIV, Curr. Opin. HIV AIDS, 14, 309, 10.1097/COH.0000000000000551 · DOI
  60. Zost, 2020, Potently neutralizing human antibodies that block SARS-CoV-2 receptor binding and protect animals, bioRxiv

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Metadata

Authors
Kreer, C., Zehner, M., Weber, T., Ercanoglu, M. S., Gieselmann, L., Rohde, C., Halwe, S., Korenkov, M., Schommers, P., Vanshylla, K., Di Cristanziano, V., Janicki, H., Brinker, R., Ashurov, A., Krähling, V., Kupke, A., Cohen-Dvashi, H., Koch, M., Eckert, J. M., Lederer, S., Pfeifer, N., Wolf, T., Vehreschild, M. J. G. T., Wendtner, C., Diskin, R., Gruell, H., Becker, S., & Klein, F.
Venue
Cell
Publisher
Elsevier BV
Published
2020-08
Volume
182
Issue
4
Pages
843-854.e12
ISSN
0092-8674
DOI
10.1016/j.cell.2020.06.044
PMC
PMC7355337
Cited by
309
References
13
Language
en
Update notices
erratum (2020-09-17)
Licence
Funders
  • Bundesministerium für Bildung und Forschung
  • Deutsches Zentrum für Infektionsforschung
  • Deutsche Forschungsgemeinschaft
  • European Research Council

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