@article{10.1172/jci.insight.150012, author = {Ester Lopez AND Ebene R. Haycroft AND Amy Adair AND Francesca L. Mordant AND Matthew T. O’Neill AND Phillip Pymm AND Samuel J. Redmond AND Wen Shi Lee AND Nicholas A. Gherardin AND Adam K. Wheatley AND Jennifer A. Juno AND Kevin J. Selva AND Samantha K. Davis AND Samantha L. Grimley AND Leigh Harty AND Damian F.J. Purcell AND Kanta Subbarao AND Dale I. Godfrey AND Stephen J. Kent AND Wai-Hong Tham AND Amy W. Chung}, journal = {JCI Insight}, publisher = {The American Society for Clinical Investigation}, title = {Simultaneous evaluation of antibodies that inhibit SARS-CoV-2 variants via multiplex assay}, year = {2021}, month = {8}, volume = {6}, url = {https://insight.jci.org/articles/view/150012}, 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.}, number = {16}, doi = {10.1172/jci.insight.150012}, url = {https://doi.org/10.1172/jci.insight.150012}, }