What question did this study set out to answer?

To systematically profile how extensive mutations across the SARS-CoV-2 spike glycoprotein alter ACE2 receptor affinity and evade neutralization by monoclonal antibodies.

April 11, 2023Cell DiscoveryOpen Access

High-throughput screening of spike variants uncovers the key residues that alter the affinity and antigenicity of SARS-CoV-2

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Authors

YLYufeng Luo SLShuo Liu JXJiguo Xue

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Overview

In vitro high-throughput screening reveals key spike mutations enhancing infectivity and antibody resistance, highlighting mechanisms driving SARS-CoV-2 immune evasion.

Key Points

To systematically profile how extensive mutations across the SARS-CoV-2 spike glycoprotein alter ACE2 receptor affinity and evade neutralization by monoclonal antibodies.
Generated a lentiviral spike variant library in a mammalian cell-surface-display system using in silico chip synthesis and site-directed saturation mutagenesis.
Enriched and isolated variant candidates via single-cell fluorescence-activated sorting.
Identified and quantified mutational effects using third-generation DNA sequencing technologies.
Spike mutations S205F, Y453F, Q493A, Q493M, Q498H, Q498Y, N501F, and N501T demonstrated a 3- to 12-fold increase in viral infectivity.
Variants Y453F, Q493A, and Q498Y exhibited at least a 10-fold resistance to monoclonal antibodies REGN10933, LY-CoV555, and REGN10987, respectively.

Cite This Study

Luo et al. (2023) studied this question.

synapsesocial.com/papers/6a8a6bad9be9d02581bdad3d https://doi.org/10.1038/s41421-023-00534-2

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April 11, 2023Cell DiscoveryOpen Access

High-throughput screening of spike variants uncovers the key residues that alter the affinity and antigenicity of SARS-CoV-2

View Full Paper

Ask AI

Bookmark

Authors

YLYufeng Luo SLShuo Liu JXJiguo Xue

Discussion

Member takes

Overview

In vitro high-throughput screening reveals key spike mutations enhancing infectivity and antibody resistance, highlighting mechanisms driving SARS-CoV-2 immune evasion.

Key Points

To systematically profile how extensive mutations across the SARS-CoV-2 spike glycoprotein alter ACE2 receptor affinity and evade neutralization by monoclonal antibodies.
Generated a lentiviral spike variant library in a mammalian cell-surface-display system using in silico chip synthesis and site-directed saturation mutagenesis.
Enriched and isolated variant candidates via single-cell fluorescence-activated sorting.
Identified and quantified mutational effects using third-generation DNA sequencing technologies.
Spike mutations S205F, Y453F, Q493A, Q493M, Q498H, Q498Y, N501F, and N501T demonstrated a 3- to 12-fold increase in viral infectivity.
Variants Y453F, Q493A, and Q498Y exhibited at least a 10-fold resistance to monoclonal antibodies REGN10933, LY-CoV555, and REGN10987, respectively.

Cite This Study

Luo et al. (2023) studied this question.

synapsesocial.com/papers/6a8a6bad9be9d02581bdad3d https://doi.org/10.1038/s41421-023-00534-2

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