ArticleNature communications2022
Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Single molecule force spectroscopy for evaluating inhibitors of SARS-CoV-2 variants of concern.European biophysics journal : EBJ · 2026Review
- Switching Spike Plasticity Shapes ACE2 Engagement Across SARS-CoV-2 Variants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Glycans Modulate the Adsorption of RBD Glycoproteins on Polarizable Surfaces.Journal of chemical information and modeling · 2026Article
- Bioinformatics and artificial intelligence in genomic data analysis: current advances and future directions.Molecular genetics and genomics : MGG · 2025Review
- Automated Label-Free Assay for Viral Detection and Inhibitor Screening via Biomembrane-Functionalized Microelectrode Arrays.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Multimodal Structural Characterization of SARS-CoV-2 Spike Variants: Spectroscopic and Computational Insights.International journal of molecular sciences · 2025Article
- Article
- Exploring the Intrinsic Structural Plasticity and Conformational Dynamics of Human Beta Coronavirus Spike Glycoproteins.Journal of chemical information and modeling · 2025Article
- Modulation of SARS-CoV-2 spike binding to ACE2 through conformational selection.Nature nanotechnology · 2025Article
- Variant-Specific Interactions at the Plasma Membrane: Heparan Sulfate's Impact on SARS-CoV-2 Binding Kinetics.Analytical chemistry · 2025Article
- The accomplices: Heparan sulfates and N-glycans foster SARS-CoV-2 spike:ACE2 receptor binding and virus priming.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mechanisms of Plasma Ozone and UV-C Sterilization of SARS-CoV-2 Explored through Atomic Force Microscopy.ACS applied materials & interfaces · 2024Article
- SARS-CoV-2 Genotyping Highlights the Challenges in Spike Protein Drift Independent of Other Essential Proteins.Microorganisms · 2024Article
- Adsorption-Driven Deformation and Footprints of the RBD Proteins in SARS-CoV-2 Variants on Biological and Inanimate Surfaces.Journal of chemical information and modeling · 2024Article
- Article
- Molecular Mechanism of Interaction between DNA Aptamer and Receptor-Binding Domain of Severe Acute Respiratory Syndrome Coronavirus 2 Variants Revealed by Steered Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2024Article
- Single-Molecule Investigation of the Binding Interface Stability of SARS-CoV-2 Variants with ACE2.ACS nanoscience Au · 2024Article
- Single-molecule force stability of the SARS-CoV-2-ACE2 interface in variants-of-concern.Nature nanotechnology · 2024Article
- Deciphering the free energy landscapes of SARS-CoV-2 wild type and Omicron variant interacting with human ACE2.The Journal of chemical physics · 2024Article
- Biophysical investigation of interactions between SARS-CoV-2 spike protein and neuropilin-1.Protein science : a publication of the Protein Society · 2023Article
Corrections and comments
- Erratum issued
Authors and funding
19 authors at 9 institutions in 6 countries.
Funding
Abstract
Recent waves of COVID-19 correlate with the emergence of the Delta and the Omicron variant. We report that the Spike trimer acts as a highly dynamic molecular caliper, thereby forming up to three tight bonds through its RBDs with ACE2 expressed on the cell surface. The Spike of both Delta and Omicron (B.1.1.529) Variant enhance and markedly prolong viral attachment to the host cell receptor ACE2, as opposed to the early Wuhan-1 isolate. Delta Spike shows rapid binding of all three Spike RBDs to three different ACE2 molecules with considerably increased bond lifetime when compared to the reference strain, thereby significantly amplifying avidity. Intriguingly, Omicron (B.1.1.529) Spike displays less multivalent bindings to ACE2 molecules, yet with a ten time longer bond lifetime than Delta. Delta and Omicron (B.1.1.529) Spike variants enhance and prolong viral attachment to the host, which likely not only increases the rate of viral uptake, but also enhances the resistance of the variants against host-cell detachment by shear forces such as airflow, mucus or blood flow. We uncover distinct binding mechanisms and strategies at single-molecule resolution, employed by circulating SARS-CoV-2 variants to enhance infectivity and viral transmission.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.