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10.1172/jci.insight.150012

http://scihub22266oqcxt.onion/10.1172/jci.insight.150012
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34251356!8409985!34251356
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suck abstract from ncbi


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pmid34251356      JCI+Insight 2021 ; 6 (16): ä
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  • Simultaneous evaluation of antibodies that inhibit SARS-CoV-2 variants via multiplex assay #MMPMID34251356
  • 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
  • JCI Insight 2021[Aug]; 6 (16): ä PMID34251356show ga
  • 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.
  • |Angiotensin-Converting Enzyme 2/metabolism[MESH]
  • |Antibodies, Neutralizing/*immunology[MESH]
  • |Antibodies, Viral/*immunology[MESH]
  • |High-Throughput Screening Assays[MESH]
  • |Humans[MESH]
  • |Immune Evasion[MESH]
  • |Mutation[MESH]


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