ArticleProceedings of the National Academy of Sciences of the United States of America2019
Affinity maturation in a human humoral response to influenza hemagglutinin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- Article
- Antigenic drift expands influenza viral escape pathways from recalled humoral immunity.Immunity · 2025Article
- Steered molecular dynamics simulation as a post-process to optimize the iBRAB-designed Fab model.Journal of computer-aided molecular design · 2024Article
- Review
- A new class of antibodies that overcomes a steric barrier to cross-group neutralization of influenza viruses.PLoS biology · 2023Article
- Germline-encoded specificities and the predictability of the B cell response.PLoS pathogens · 2023Article
- Structural basis for breadth development in the HIV-1 V3-glycan targeting DH270 antibody clonal lineage.Nature communications · 2023Article
- Article
- Computational identification of HCV neutralizing antibodies with a common HCDR3 disulfide bond motif in the antibody repertoires of infected individuals.Nature communications · 2022Review
- Complexity of Viral Epitope Surfaces as Evasive Targets for Vaccines and Therapeutic Antibodies.Frontiers in immunology · 2022Review
- SARS-CoV-2 Serologic Assays Dependent on Dual-Antigen Binding Demonstrate Diverging Kinetics Relative to Other Antibody Detection Methods.Journal of clinical microbiology · 2021Article
- Affinity Tag Coating Enables Reliable Detection of Antigen-Specific B Cells in Immunospot Assays.Cells · 2021Article
- A Prevalent Focused Human Antibody Response to the Influenza Virus Hemagglutinin Head Interface.mBio · 2021Article
- High-resolution asymmetric structure of a Fab-virus complex reveals overlap with the receptor binding site.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- B Cell Responses against Influenza Viruses: Short-Lived Humoral Immunity against a Life-Long Threat.Viruses · 2021Review
- Progress toward improved understanding of antibody maturation.Current opinion in structural biology · 2021Review
- Structure-Guided Molecular Grafting of a Complex Broadly Neutralizing Viral Epitope.ACS infectious diseases · 2020Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Affinity maturation of the B cell antigen receptor (BCR) is a conserved and crucial component of the adaptive immune response. BCR lineages, inferred from paired heavy- and light-chain sequences of rearranged Ig genes from multiple descendants of the same naive B cell precursor (the lineages' unmutated common ancestor, "UCA"), make it possible to reconstruct the underlying somatic evolutionary history. We present here an extensive structural and biophysical analysis of a lineage of BCRs directed against the receptor binding site (RBS) of subtype H1 influenza virus hemagglutinin (HA). The lineage includes 8 antibodies detected directly by sequencing, 3 in 1 principal branch and 5 in the other. When bound to HA, the heavy-chain third complementarity determining region (HCDR3) fits with an invariant pose into the RBS, but in each of the 2 branches, the rest of the Fab reorients specifically, from its position in the HA-bound UCA, about a hinge at the base of HCDR3. New contacts generated by the reorientation compensate for contacts lost as the H1 HA mutated during the time between the donor's initial exposure and the vaccination that preceded sampling. Our data indicate that a "pluripotent" naive response differentiated, in each branch, into 1 of its possible alternatives. This property of naive BCRs and persistence of multiple branches of their progeny lineages can offer broader protection from evolving pathogens than can a single, linear pathway of somatic mutation.
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