ArticleACS central science2021
Probing Affinity, Avidity, Anticooperativity, and Competition in Antibody and Receptor Binding to the SARS-CoV-2 Spike by Single Particle Mass Analyses.
Article in ACS central science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- Complete enzyme clustering enhances coenzyme Q biosynthesis via substrate channeling.Nature communications · 2026Article
- Mass Photometry Reveals Distinct ACE2 Binding Stoichiometries across SARS-CoV-2 Omicron Subvariants.The journal of physical chemistry. B · 2026Article
- Screening pertactin-specific antibodies and evaluating competitive epitope recognition by native mass spectrometry.Chemical science · 2026Article
- IgG-Bridging-Seeded Synergistic Aggregation of SARS-CoV-2 Spikes Underlies Potent Neutralization by a Low-Affinity Antibody.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Bispecific antibodies against the hepatitis C virus E1E2 envelope glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Current and Near-Future Technologies to Quantify Nanoparticle Therapeutic Loading Efficiency and Surface Coating Efficiency with Targeted Moieties.Bioengineering (Basel, Switzerland) · 2025Review
- Structural and virological identification of neutralizing antibody footprint provides insights into therapeutic antibody design against SARS-CoV-2 variants.Communications biology · 2025Article
- Broadening sarbecovirus neutralization with bispecific antibodies combining distinct conserved targets on the receptor binding domain.Human vaccines & immunotherapeutics · 2024Article
- Exploring distinct modes of inter-spike cross-linking for enhanced neutralization by SARS-CoV-2 antibodies.Nature communications · 2024Article
- Oligomerization-driven avidity correlates with SARS-CoV-2 cellular binding and inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A paintbrush for delivery of nanoparticles and molecules to live cells with precise spatiotemporal control.Nature methods · 2024Article
- Immunocomplexed Antigen Capture and Identification by Native Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023Article
- Orbitrap-Based Mass and Charge Analysis of Single Molecules.Accounts of chemical research · 2023Article
- Bispecific antibodies combine breadth, potency, and avidity of parental antibodies to neutralize sarbecoviruses.iScience · 2023Article
- Uncovering the Role ofJournal of the American Chemical Society · 2023Article
- Charge detection mass spectrometry for the analysis of viruses and virus-like particles.Essays in biochemistry · 2023Article
- Avidity engineering of human heavy-chain-only antibodies mitigates neutralization resistance of SARS-CoV-2 variants.Frontiers in immunology · 2023Article
- Discriminating cross-reactivity in polyclonal IgG1 responses against SARS-CoV-2 variants of concern.Nature communications · 2022Article
- Review
- Structural and Computational Studies of the SARS-CoV-2 Spike Protein Binding Mechanisms with Nanobodies: From Structure and Dynamics to Avidity-Driven Nanobody Engineering.International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Determining how antibodies interact with the spike (S) protein of the SARS-CoV-2 virus is critical for combating COVID-19. Structural studies typically employ simplified, truncated constructs that may not fully recapitulate the behavior of the original complexes. Here, we combine two single particle mass analysis techniques (mass photometry and charge-detection mass spectrometry) to enable the measurement of full IgG binding to the trimeric SARS-CoV-2 S ectodomain. Our experiments reveal that antibodies targeting the S-trimer typically prefer stoichiometries lower than the symmetry-predicted 3:1 binding. We determine that this behavior arises from the interplay of steric clashes and avidity effects that are not reflected in common antibody constructs (i.e., Fabs). Surprisingly, these substoichiometric complexes are fully effective at blocking ACE2 binding despite containing free receptor binding sites. Our results highlight the importance of studying antibody/antigen interactions using complete, multimeric constructs and showcase the utility of single particle mass analyses in unraveling these complex interactions.
Identifiers
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Registered trials
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.