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Basic Characteristics of Mutations
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Mutation Site
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Q493L |
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Mutation Site Sentence
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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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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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RBD |
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Standardized Encoding Gene
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S
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Genotype/Subtype
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- |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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COVID-19
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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Australia |
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Literature Information
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PMID
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34251356
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Title
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Simultaneous evaluation of antibodies that inhibit SARS-CoV-2 variants via multiplex assay
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Author
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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
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Journal
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JCI insight
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Journal Info
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2021 Aug 23;6(16):e150012
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Abstract
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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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Sequence Data
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-
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