ArticleCell2022
Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2.
Article in Cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 306 papers.
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Who cites it
306 citing papers in PubMed.
- Disulfide bonds stabilize the SARS-CoV-2 RBD and preserve binding to ACE2 following thermal denaturation.Bioscience reports · 2026Article
- An inverse-protein-folding pre-trained model for predicting the mutational effects in protein-protein interactions.iScience · 2026Article
- Extracellular Vesicles as Molecular Regulators of Viral Infection: Implications for COVID-19 and Future Viral Pandemics.Current issues in molecular biology · 2026Review
- Dual engagement of Spike and ACE2 by annexin A5 contributes to pleiotropic SARS-CoV-2 inhibition.Scientific reports · 2026Article
- Molecular Dynamics and Solvated Interaction Energy Prioritize Cannabidiol and Cannabinol as Variant-Spanning SARS-CoV-2 RBD-ACE2 Interface Blockers.Molecules (Basel, Switzerland) · 2026Article
- Article
- Machine learning-guided rational engineering of ACE2-derived peptides for broad-spectrum neutralization of SARS-CoV-2 variants.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2026Article
- Computational and experimental identification of potential neutralizing peptides derived from human ACE2 against SARS-CoV-2 infection.Journal of virology · 2026Article
- The role of receptor binding and immunity in SARS-CoV-2 fitness landscape: A modeling study.iScience · 2026Article
- Natural Selection-Guided ACE2-Targeted Molecular Imaging: A New Paradigm for PET Tracer Development.Chemical & biomedical imaging · 2026Article
- Recombinant RBD-based subunit vaccines incorporating high-frequency mutation sites elicit cross-immunity and robust protection against SARS-CoV-2.Frontiers in microbiology · 2026Article
- Computational Optimization of CRISPR-Cas13a sgRNAs Targeting the SARS-CoV-2 Spike Gene for SHERLOCK-Based Diagnostics.Evolutionary bioinformatics online · 2026Article
- Seq2Bind webserver for binding site prediction from sequences using fine-tuned protein language models.NAR genomics and bioinformatics · 2025Article
- P selectin promotes SARS-CoV-2 interactions with platelets and the endothelium.The Journal of clinical investigation · 2025Article
- SARS-CoV-2 Evolution in Humans Enables Its Transmission to Nonhuman Primates.Molecular biology and evolution · 2025Article
- Integrated antibody language model accelerates IgG screening and design for broad-spectrum antiviral therapy.iScience · 2025Article
- Molecular mechanisms of SARS-CoV-2 entry: implications for biomedical strategies.Microbiology and molecular biology reviews : MMBR · 2025Review
- Interaction Between Heparan Sulfate Oligosaccharide and the Receptor-Binding Domain of the Wild-Type and Omicron Variant of the SARS-CoV-2 Spike Protein.Biomolecules · 2025Article
- Development of a Liposome-Based Serological Assay for SARS-CoV-2 Variants with Special Emphasis on Coupling Chemistries Required to Maintain Protein Antigenicity.Analytical chemistry · 2025Article
- Rapid Discovery of Potent Neutralizing Antibodies against SARS-CoV-2 through Directed Evolution of SARS-CoV-1 Antibodies.Molecular pharmaceutics · 2025Article
246 more citing papers are in PubMed but not listed here.
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Authors and funding
21 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The coronavirus disease 2019 (COVID-19) pandemic continues worldwide with many variants arising, some of which are variants of concern (VOCs). A recent VOC, omicron (B.1.1.529), which obtains a large number of mutations in the receptor-binding domain (RBD) of the spike protein, has risen to intense scientific and public attention. Here, we studied the binding properties between the human receptor ACE2 (hACE2) and the VOC RBDs and resolved the crystal and cryoelectron microscopy structures of the omicron RBD-hACE2 complex as well as the crystal structure of the delta RBD-hACE2 complex. We found that, unlike alpha, beta, and gamma, omicron RBD binds to hACE2 at a similar affinity to that of the prototype RBD, which might be due to compensation of multiple mutations for both immune escape and transmissibility. The complex structures of omicron RBD-hACE2 and delta RBD-hACE2 reveal the structural basis of how RBD-specific mutations bind to hACE2.
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