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Simultaneous evaluation of antibodies that inhibit SARS-CoV-2 variants via multiplex assay.
Lopez, Ester; Haycroft, Ebene R; Adair, Amy; Mordant, Francesca L; O'Neill, Matthew T; Pymm, Phillip; Redmond, Samuel J; Lee, Wen Shi; Gherardin, Nicholas A; Wheatley, Adam K; Juno, Jennifer A; Selva, Kevin J; Davis, Samantha K; Grimley, Samantha L; Harty, Leigh; Purcell, Damian Fj; Subbarao, Kanta; Godfrey, Dale I; Kent, Stephen J; Tham, Wai-Hong; Chung, Amy W.
  • Lopez E; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Haycroft ER; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Adair A; The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia.
  • Mordant FL; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • O'Neill MT; The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia.
  • Pymm P; The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia.
  • Redmond SJ; Australian Research Council Centre for Excellence in Convergent Bio-Nano Science & Technology, The University of Melbourne, Parkville, Victoria, Australia.
  • Lee WS; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Gherardin NA; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Wheatley AK; The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia.
  • Juno JA; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Selva KJ; Australian Research Council Centre of Excellence for Advanced Molecular Imaging, The University of Melbourne, Melbourne, Victoria, Australia.
  • Davis SK; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Grimley SL; Australian Research Council Centre for Excellence in Convergent Bio-Nano Science & Technology, The University of Melbourne, Parkville, Victoria, Australia.
  • Harty L; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Purcell DF; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Subbarao K; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Godfrey DI; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Kent SJ; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Tham WH; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  • Chung AW; Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
JCI Insight ; 6(16)2021 08 23.
Article in English | MEDLINE | ID: covidwho-1305530
ABSTRACT
The SARS-CoV-2 receptor binding domain (RBD) is both the principal target of neutralizing antibodies and one of the most rapidly evolving domains, which can result in the emergence of immune escape mutations, limiting the effectiveness of vaccines and antibody therapeutics. To facilitate surveillance, we developed a rapid, high-throughput, multiplex assay able to assess the inhibitory response of antibodies to 24 RBD natural variants simultaneously. We demonstrate how this assay can be implemented as a rapid surrogate assay for functional cell-based serological methods to measure the SARS-CoV-2 neutralizing capacity of antibodies at the angiotensin-converting enzyme 2-RBD (ACE2-RBD) interface. We describe the enhanced affinity of RBD variants N439K, S477N, Q493L, S494P, and N501Y to the ACE2 receptor and demonstrate the ability of this assay to bridge a major gap for SARS-CoV-2 research, informing selection of complementary monoclonal antibody candidates and the rapid identification of immune escape to emerging RBD variants following vaccination or natural infection.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Antibodies, Neutralizing / SARS-CoV-2 / Antibodies, Viral Type of study: Experimental Studies Topics: Vaccines / Variants Limits: Humans Language: English Year: 2021 Document Type: Article Affiliation country: Jci.insight.150012

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Antibodies, Neutralizing / SARS-CoV-2 / Antibodies, Viral Type of study: Experimental Studies Topics: Vaccines / Variants Limits: Humans Language: English Year: 2021 Document Type: Article Affiliation country: Jci.insight.150012