ArticleSignal transduction and targeted therapy2021
S19W, T27W, and N330Y mutations in ACE2 enhance SARS-CoV-2 S-RBD binding toward both wild-type and antibody-resistant viruses and its molecular basis.
Article in Signal transduction and targeted therapy, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- An IgG-like fusion protein comprising an anti-spike S2 antibody and ACE2 exhibits potent and broad neutralization against SARS-CoV-2 and variants of concern.Antibody therapeutics · 2026Article
- Optimized ACE2-Fc fusion proteins with picomolar neutralization activity against highly evolved SARS-CoV-2 variants.Protein science : a publication of the Protein Society · 2026Article
- multiSMD - A Python Toolset for Multidirectional Steered Molecular Dynamics.Journal of chemical information and modeling · 2025Article
- A combinatorial and computational Tandem approach towards a universal therapeutics against ACE2-mediated coronavirus infections.iScience · 2025Article
- Structural basis and mode of action for two broadly neutralizing nanobodies targeting the highly conserved spike stem-helix of sarbecoviruses including SARS-CoV-2 and its variants.PLoS pathogens · 2025Article
- XBB.1.16-RBD-based trimeric protein vaccine can effectively inhibit XBB.1.16-included XBB subvariant infection.MedComm · 2024Article
- A Natural Bioactive Peptide fromInternational journal of molecular sciences · 2024Article
- Understanding COVID-19-associated endothelial dysfunction: role of PIEZO1 as a potential therapeutic target.Frontiers in immunology · 2024Review
- Development of a bispecific nanobody conjugate broadly neutralizes diverse SARS-CoV-2 variants and structural basis for its broad neutralization.PLoS pathogens · 2023Article
- A Suitable Membrane Distance Regulated by the RBD_ACE2 Interaction is Critical for SARS-CoV-2 Spike-Mediated Viral Invasion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Deep-learning-enabled protein-protein interaction analysis for prediction of SARS-CoV-2 infectivity and variant evolution.Nature medicine · 2023Article
- A computationally designed ACE2 decoy has broad efficacy against SARS-CoV-2 omicron variants and related viruses in vitro and in vivo.Communications biology · 2023Article
- Convergent evolution of SARS-CoV-2 Omicron subvariants leading to the emergence of BQ.1.1 variant.Nature communications · 2023Article
- Optimizing variant-specific therapeutic SARS-CoV-2 decoys using deep-learning-guided molecular dynamics simulations.Scientific reports · 2023Article
- Article
- Glycan masking of a non-neutralising epitope enhances neutralising antibodies targeting the RBD of SARS-CoV-2 and its variants.Frontiers in immunology · 2023Article
- An engineered 5-helix bundle derived from SARS-CoV-2 S2 pre-binds sarbecoviral spike at both serological- and endosomal-pH to inhibit virus entry.Emerging microbes & infections · 2022Article
- Angiotensin-Converting Enzyme 2-Based Biosensing Modalities and Devices for Coronavirus Detection.Biosensors · 2022Review
- Engineering ACE2 decoy receptors to combat viral escapability.Trends in pharmacological sciences · 2022Review
- A self-assembled trimeric protein vaccine induces protective immunity against Omicron variant.Nature communications · 2022Article
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Abstract
SARS-CoV-2 recognizes, via its spike receptor-binding domain (S-RBD), human angiotensin-converting enzyme 2 (ACE2) to initiate infection. Ecto-domain protein of ACE2 can therefore function as a decoy. Here we show that mutations of S19W, T27W, and N330Y in ACE2 could individually enhance SARS-CoV-2 S-RBD binding. Y330 could be synergistically combined with either W19 or W27, whereas W19 and W27 are mutually unbeneficial. The structures of SARS-CoV-2 S-RBD bound to the ACE2 mutants reveal that the enhanced binding is mainly contributed by the van der Waals interactions mediated by the aromatic side-chains from W19, W27, and Y330. While Y330 and W19/W27 are distantly located and devoid of any steric interference, W19 and W27 are shown to orient their side-chains toward each other and to cause steric conflicts, explaining their incompatibility. Finally, using pseudotyped SARS-CoV-2 viruses, we demonstrate that these residue substitutions are associated with dramatically improved entry-inhibition efficacy toward both wild-type and antibody-resistant viruses. Taken together, our biochemical and structural data have delineated the basis for the elevated S-RBD binding associated with S19W, T27W, and N330Y mutations in ACE2, paving the way for potential application of these mutants in clinical treatment of COVID-19.
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