ArticleCell reports2021
Polyclonal epitope mapping reveals temporal dynamics and diversity of human antibody responses to H5N1 vaccination.
Article in Cell reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 62 citations in OpenAlex.
- Design of Epitope-Focused Vaccines via Epitope Cleavage.ACS central science · 2026Article
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- The buried S2 apex of SARS-CoV-2 spike elicits an immunodominant germline-restricted public antibody response.bioRxiv : the preprint server for biology · 2026Article
- Cryo-EM structures of antibodies elicited by germline-targeting HIV MPER epitope scaffolds.Cell reports · 2026Article
- Innovative Single-Cell Sequencing Techniques for B cell Analysis and Their Implications for Rational HIV-1 Vaccine Design.Current HIV research · 2026Review
- Resistance Mutations to Broadly Neutralizing Antibodies Destabilize Hemagglutinin and Attenuate H1N1 Influenza Virus.Viruses · 2025Article
- Structural and immunological characterization of the H3 influenza hemagglutinin during antigenic drift.Nature communications · 2025Article
- Article
- Microfluidics combined with electron microscopy for rapid and high-throughput mapping of antibody-viral glycoprotein complexes.Nature biomedical engineering · 2025Article
- Single-dose avian influenza A(H5N1) Clade 2.3.4.4b hemagglutinin-Matrix-MNature communications · 2025Article
- Article
- Article
- Structural mapping of polyclonal IgG responses to HA after influenza virus vaccination or infection.mBio · 2025Article
- Structures and functions of the limited natural polyclonal antibody response to parvovirus infection.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Human naïve B cells recognize prepandemic influenza virus hemagglutinins.Science immunology · 2025Article
- Factors determining the outcomes of immune imprinting after repeated orthoflavivirus infections.Frontiers in immunology · 2025Review
- Antibodies and cryptographic hash functions: quantifying the specificity paradox.Frontiers in immunology · 2025Article
- Defining bottlenecks and opportunities for Lassa virus neutralization by structural profiling of vaccine-induced polyclonal antibody responses.Cell reports · 2024Article
- Vaccine design via antigen reorientation.Nature chemical biology · 2024Article
- Full-length MSP1 is a major target of protective immunity after controlled human malaria infection.Life science alliance · 2024Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Novel influenza A virus (IAV) strains elicit recall immune responses to conserved epitopes, making them favorable antigenic choices for universal influenza virus vaccines. Evaluating these immunogens requires a thorough understanding of the antigenic sites targeted by the polyclonal antibody (pAb) response, which single-particle electron microscopy (EM) can sensitively detect. In this study, we employ EM polyclonal epitope mapping (EMPEM) to extensively characterize the pAb response to hemagglutinin (HA) after H5N1 immunization in humans. Cross-reactive pAbs originating from memory B cells immediately bound the stem of HA and persisted for more than a year after vaccination. In contrast, de novo pAb responses to multiple sites on the head of HA, targeting previously determined key neutralizing sites on H5 HA, expanded after the second immunization and waned quickly. Thus, EMPEM provides a robust tool for comprehensively tracking the specificity and durability of immune responses elicited by novel universal influenza vaccine candidates.
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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.