ArticleCell reports methods2023
Increasing sensitivity of antibody-antigen interactions using photo-cross-linking.
Article in Cell reports methods, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed.
- Structural serology of polyclonal antibody responses to mRNA-1273 and NVX-CoV2373 COVID-19 vaccines.Cell reports · 2025Trial
- Structural and functional characterization of the antigenicity of influenza A virus hemagglutinin subtype H15.Cell reports · 2026Article
- Structural and immunological characterization of the H3 influenza hemagglutinin during antigenic drift.Nature communications · 2025Article
- Microfluidics combined with electron microscopy for rapid and high-throughput mapping of antibody-viral glycoprotein complexes.Nature biomedical engineering · 2025Article
- Immunofocusing on the conserved fusion peptide of HIV envelope glycoprotein in rhesus macaques.NPJ vaccines · 2025Article
- Immunofocusing on the conserved fusion peptide of HIV envelope glycoprotein in rhesus macaques.bioRxiv : the preprint server for biology · 2025Article
- Determining T-cell receptor binding orientation and Peptide-HLA interactions using cross-linking mass spectrometry.The Journal of biological chemistry · 2025Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Understanding antibody-antigen interactions in a polyclonal immune response in humans and animal models is critical for rational vaccine design. Current approaches typically characterize antibodies that are functionally relevant or highly abundant. Here, we use photo-cross-linking and single-particle electron microscopy to increase antibody detection and unveil epitopes of low-affinity and low-abundance antibodies, leading to a broader structural characterization of polyclonal immune responses. We employed this approach across three different viral glycoproteins and showed increased sensitivity of detection relative to currently used methods. Results were most noticeable in early and late time points of a polyclonal immune response. Additionally, the use of photo-cross-linking revealed intermediate antibody binding states and demonstrated a distinctive way to study antibody binding mechanisms. This technique can be used to structurally characterize the landscape of a polyclonal immune response of patients in vaccination or post-infection studies at early time points, allowing for rapid iterative design of vaccine immunogens.
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Registered trials
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