Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The molecular reach of antibodies crucially underpins their viral neutralisation capacity

2 Jan 2025

Abstract excerpt

Key functions of antibodies, such as viral neutralisation, depend on high-affinity binding. However, viral neutralisation poorly correlates with antigen affinity for reasons that have been unclear. Here, we use a new mechanistic model of bivalent binding to study >45 patient-isolated IgG1 antibodies interacting with SARS-CoV-2 RBD surfaces. The model provides the standard monovalent affinity/kinetics and new...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Monoclonal and Polyclonal Antibodies Research
Share to Protein purification and stability
Share to SARS-CoV-2 and COVID-19 Research

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 39746910
DOI: 10.1038/s41467-024-54916-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 23 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The molecular reach of antibodies crucially underpins their viral neutralisation capacityPMID 39746910Read ↗

Microfluidic antibody profiling after repeated SARS-CoV-2 vaccination links antibody affinity and concentration to impaired immunity and variant escape in patients on anti-CD-20 therapySemantic proximity Read ↗

Sagacious Epitope Selection for Vaccines, and Both Antibody-Based Therapeutics and Diagnostics: Tips From Virology and Oncology<strong> </strong>Semantic proximity Read ↗

The Influence of Variable-Heavy (V <sub>H</sub> ) Chain Families on IgG <sub>2</sub> , <sub>3</sub> , <sub>4</sub> on FcγRs and Antibody Superantigens Protein G and L Binding using Biolayer InterferometrySemantic proximity Read ↗

Antibody avidity and multi-specificity combined to confer protection against SARS-CoV-2 and resilience against viral escapeSemantic proximity Read ↗

Dissecting binding and immune evasion mechanisms for ultrapotent Class I and Class 4/1 neutralizing antibodies of SARS-CoV-2 spike protein using a multi-pronged computational approach: neutral frustration architecture of binding interfaces and immune escape hotspots drives adaptive evolution.Semantic proximity Read ↗

Structural Adaptability of IgA and IgM Supports Broad SARS-CoV-2 Variant Neutralization.Semantic proximity Read ↗

Structural basis for breadth development in a HIV-1 neutralizing antibodySemantic proximity Read ↗

Molecular Mechanism for Antibody-Dependent Enhancement of Coronavirus EntrySemantic proximity Read ↗

A highly potent human antibody neutralizes dengue virus serotype 3 by binding across three surface proteins.Semantic proximity Read ↗

Understanding the complementarity and plasticity of antibody–antigen interfacesSemantic proximity Read ↗

Profiling the Biophysical Developability Properties of Common IgG1 Fc Effector Silencing VariantsSemantic proximity Read ↗

A Comprehensive Mathematical Model of Avidity in Cytokine SignalingSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.