ArticleAllergy2022
Molecular definition of severe acute respiratory syndrome coronavirus 2 receptor-binding domain mutations: Receptor affinity versus neutralization of receptor interaction.
Article in Allergy, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Impact of SARS-CoV-2 RBM Mutations N501Y and E484K on ACE2 Binding: A Combined Computational and Experimental Study.International journal of molecular sciences · 2025Article
- Article
- Protein-Protein Binding Kinetics by Biolayer Interferometry.Advances in experimental medicine and biology · 2024Article
- Facile electrochemical affinity measurements of small and large molecules.RSC advances · 2023Article
- Recent developments in the immunopathology of COVID-19.Allergy · 2023Review
- Vaccination using mutated receptor binding domains of SARS-CoV-2: Evidence for partial immune escape but not serotype formation.Frontiers in immunology · 2023Article
- Enhanced virulence and waning vaccine-elicited antibodies account for breakthrough infections caused by SARS-CoV-2 delta and beyond.iScience · 2022Article
- Efficacy and impact of SARS-CoV-2 vaccination on cancer treatment for breast cancer patients: a multi-center prospective observational study.Breast cancer research and treatment · 2022Observational
- Article
- Designing and characterization of a SARS-CoV-2 immunogen with receptor binding motif grafted on a protein scaffold: An epitope-focused vaccine approach.International journal of biological macromolecules · 2022Article
- Increased receptor affinity of SARS-CoV-2: a new immune escape mechanism.NPJ vaccines · 2022Article
- Functional mutations of SARS-CoV-2: implications to viral transmission, pathogenicity and immune escape.Chinese medical journal · 2022Article
- Interfering effects on the bioactivities of several key proteins of COVID-19/variants in diabetes by compounds from Lianqiao leaves: In silico and in vitro analyses.International journal of biological macromolecules · 2022Article
- Increased Receptor Affinity and Reduced Recognition by Specific Antibodies Contribute to Immune Escape of SARS-CoV-2 Variant Omicron.Vaccines · 2022Article
- Omicron: A SARS-CoV-2 variant of real concern.Allergy · 2022Article
- Review
- Early Genomic, Epidemiological, and Clinical Description of the SARS-CoV-2 Omicron Variant in Mexico City.Viruses · 2022Article
- Induction of Broadly Cross-Reactive Antibodies by Displaying Receptor Binding Domains of SARS-CoV-2 on Virus-like Particles.Vaccines · 2022Article
- Article
- Article
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Authors and funding
7 authors.
Funding
Abstract
backgroundSeveral new variants of SARS-CoV-2 have emerged since fall 2020 which have multiple mutations in the receptor-binding domain (RBD) of the spike protein. It is unclear which mutations affect receptor affinity versus immune recognition.
methodsWe produced wild type RBD, RBD with single mutations (E484K, K417N, or N501Y) or with all three mutations combined and tested their binding to ACE2 by biolayer interferometry (BLI). The ability of convalescent sera to recognize RBDs and block their interaction with ACE2 was tested as well.
resultsWe demonstrated that single mutation N501Y increased binding affinity to ACE2 but did not strongly affect its recognition by convalescent sera. In contrast, single mutation E484K had almost no impact on the binding kinetics, but essentially abolished recognition of RBD by convalescent sera. Interestingly, combining mutations E484K, K417N, and N501Y resulted in a RBD with both features: enhanced receptor binding and abolished immune recognition.
conclusionsOur data demonstrate that single mutations either affect receptor affinity or immune recognition while triple mutant RBDs combine both features.
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