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Basic Characteristics of Mutations
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Mutation Site
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P132H |
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Mutation Site Sentence
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These VOC/VOI carry prevalent mutations at varying frequencies in the Mpro specifically for: alpha, beta, gamma (K90R), lambda (G15S) and omicron (P132H). |
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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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Mpro |
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Standardized Encoding Gene
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ORF1a
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Genotype/Subtype
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Omicron |
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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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- |
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Literature Information
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PMID
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35461811
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Title
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Structural basis for the in vitro efficacy of nirmatrelvir against SARS-CoV-2 variants
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Author
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Greasley SE,Noell S,Plotnikova O,Ferre R,Liu W,Bolanos B,Fennell K,Nicki J,Craig T,Zhu Y,Stewart AE,Steppan CM
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Journal
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The Journal of biological chemistry
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Journal Info
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2022 Jun;298(6):101972
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Abstract
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The COVID-19 pandemic continues to be a public health threat with emerging variants of SARS-CoV-2. Nirmatrelvir (PF-07321332) is a reversible, covalent inhibitor targeting the main protease (M(pro)) of SARS-CoV-2 and the active protease inhibitor in PAXLOVID (nirmatrelvir tablets and ritonavir tablets). However, the efficacy of nirmatrelvir is underdetermined against evolving SARS-CoV-2 variants. Here, we evaluated the in vitro catalytic activity and potency of nirmatrelvir against the M(pro) of prevalent variants of concern (VOCs) or variants of interest (VOIs): Alpha (alpha, B.1.1.7), Beta (beta, B.1.351), Delta (delta, B1.617.2), Gamma (gamma, P.1), Lambda (lambda, B.1.1.1.37/C37), Omicron (omicron, B.1.1.529), as well as the original Washington or wildtype strain. These VOCs/VOIs carry prevalent mutations at varying frequencies in the M(pro) specifically for alpha, beta, gamma (K90R), lambda (G15S), and omicron (P132H). In vitro biochemical enzymatic assay characterization of the enzyme kinetics of the mutant M(pros) demonstrates that they are catalytically comparable to wildtype. We found that nirmatrelvir has similar potency against each mutant M(pro) including P132H that is observed in the Omicron variant with a Ki of 0.635 nM as compared to a Ki of 0.933 nM for wildtype. The molecular basis for these observations were provided by solution-phase structural dynamics and structural determination of nirmatrelvir bound to the omicron, lambda, and beta M(pro) at 1.63 to 2.09 A resolution. These in vitro data suggest that PAXLOVID has the potential to maintain plasma concentrations of nirmatrelvir many-fold times higher than the amount required to stop the SARS-CoV-2 VOC/VOI, including Omicron, from replicating in cells.
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Sequence Data
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-
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