Simultaneous evaluation of antibodies that inhibit SARS-CoV-2 variants via multiplex assay
- Author(s)
- Lopez, E; Haycroft, ER; Adair, A; Mordant, FL; O'Neill, MT; Pymm, P; Redmond, SJ; Lee, WS; Gherardin, NA; Wheatley, AK; Juno, JA; Selva, KJ; Davis, SK; Grimley, SL; Harty, L; Purcell, DF; Subbarao, K; Godfrey, DI; Kent, SJ; Tham, WH; Chung, AW;
- Journal Title
- JCI insight
- Publication Type
- epub ahead of print
- 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 neutralising capacity of antibodies at the 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.
- Research Division(s)
- Infectious Diseases And Immune Defence
- PubMed ID
- 34251356
- Publisher's Version
- https://doi.org/10.1172/jci.insight.150012
- Open Access at Publisher's Site
https://doi.org/10.1172/jci.insight.150012- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2021-07-20 11:18:11
Last Modified: 2021-07-20 12:51:36