| Literature DB >> 33707427 |
Federico Bertoglio1, Doris Meier1, Nora Langreder1, Stephan Steinke1, Ulfert Rand2, Luca Simonelli3, Philip Alexander Heine1, Rico Ballmann1, Kai-Thomas Schneider1, Kristian Daniel Ralph Roth1, Maximilian Ruschig1, Peggy Riese1,2, Kathrin Eschke2, Yeonsu Kim2, Dorina Schäckermann1, Mattia Pedotti3, Philipp Kuhn4, Susanne Zock-Emmenthal5, Johannes Wöhrle6, Normann Kilb6, Tobias Herz6, Marlies Becker1, Martina Grasshoff7, Esther Veronika Wenzel1, Giulio Russo1, Andrea Kröger7, Linda Brunotte8, Stephan Ludwig8, Viola Fühner1, Stefan Daniel Krämer6, Stefan Dübel1, Luca Varani9, Günter Roth10, Luka Čičin-Šain11,12, Maren Schubert13, Michael Hust14.
Abstract
COVID-19 is a severe acute respiratory disease caused by SARS-CoV-2, a new recently emerged sarbecovirus. This virus uses the human ACE2 enzyme as receptor for cell entry, recognizing it with the receptor binding domain (RBD) of the S1 subunit of the viral spike protein. We present the use of phage display to select anti-SARS-CoV-2 spike antibodies from the human naïve antibody gene libraries HAL9/10 and subsequent identification of 309 unique fully human antibodies against S1. 17 antibodies are binding to the RBD, showing inhibition of spike binding to cells expressing ACE2 as scFv-Fc and neutralize active SARS-CoV-2 virus infection of VeroE6 cells. The antibody STE73-2E9 is showing neutralization of active SARS-CoV-2 as IgG and is binding to the ACE2-RBD interface. Thus, universal libraries from healthy human donors offer the advantage that antibodies can be generated quickly and independent from the availability of material from recovering patients in a pandemic situation.Entities:
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Year: 2021 PMID： 33707427 DOI： 10.1038/s41467-021-21609-2
Source DB: PubMed Journal: Nat Commun ISSN： 2041-1723 Impact factor: 14.919