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Basic Characteristics of Mutations
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Mutation Site
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D614G |
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Mutation Site Sentence
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Furthermore,W25 potently neutralizes SARS-CoV-2 wild type and the D614G variant with IC50 values in the nanomolar range,demonstrating its potential as antiviral agent. |
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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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Standardized Encoding Gene
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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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Cell line
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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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33558635
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Title
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Potent neutralization of clinical isolates of SARS-CoV-2 D614 and G614 variants by a monomeric, sub-nanomolar affinity nanobody
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Author
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Valenzuela Nieto G,Jara R,Watterson D,Modhiran N,Amarilla AA,Himelreichs J,Khromykh AA,Salinas-Rebolledo C,Pinto T,Cheuquemilla Y,Margolles Y,Lopez Gonzalez Del Rey N,Miranda-Chacon Z,Cuevas A,Berking A,Deride C,Gonzalez-Moraga S,Mancilla H,Maturana D,Langer A,Toledo JP,Muller A,Uberti B,Krall P,Ehrenfeld P,Blesa J,Chana-Cuevas P,Rehren G,Schwefel D,Fernandez LA,Rojas-Fernandez A
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Journal
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Scientific reports
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Journal Info
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2021 Feb 8;11(1):3318
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Abstract
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Despite unprecedented global efforts to rapidly develop SARS-CoV-2 treatments, in order to reduce the burden placed on health systems, the situation remains critical. Effective diagnosis, treatment, and prophylactic measures are urgently required to meet global demand: recombinant antibodies fulfill these requirements and have marked clinical potential. Here, we describe the fast-tracked development of an alpaca Nanobody specific for the receptor-binding-domain (RBD) of the SARS-CoV-2 Spike protein with potential therapeutic applicability. We present a rapid method for nanobody isolation that includes an optimized immunization regimen coupled with VHH library E. coli surface display, which allows single-step selection of Nanobodies using a simple density gradient centrifugation of the bacterial library. The selected single and monomeric Nanobody, W25, binds to the SARS-CoV-2 S RBD with sub-nanomolar affinity and efficiently competes with ACE-2 receptor binding. Furthermore, W25 potently neutralizes SARS-CoV-2 wild type and the D614G variant with IC50 values in the nanomolar range, demonstrating its potential as antiviral agent.
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Sequence Data
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-
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