ArticleeLife2017
The structure of a LAIR1-containing human antibody reveals a novel mechanism of antigen recognition.
Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 18 citations in OpenAlex.
- A new mechanism of antibody diversity: formation of the natural antibodies containing LAIR1 and LILRB1 extracellular domains.Antibody therapeutics · 2024Review
- Variable Surface Antigens ofProtein and peptide letters · 2024Review
- Antibody Display Technology (ADbody) to Present Challenging and Unstable Target Proteins on Antibodies.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Impact of structural modifications of IgG antibodies on effector functions.Frontiers in immunology · 2023Review
- Mechanisms for Host Immune Evasion Mediated byFrontiers in immunology · 2022Review
- Lasso-grafting of macrocyclic peptide pharmacophores yields multi-functional proteins.Nature communications · 2021Article
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Antibodies against Plasmodium falciparum malaria at the molecular level.Nature reviews. Immunology · 2019Review
- Breaking the law: unconventional strategies for antibody diversification.Nature reviews. Immunology · 2019Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
Abstract
Antibodies are critical components of the human adaptive immune system, providing versatile scaffolds to display diverse antigen-binding surfaces. Nevertheless, most antibodies have similar architectures, with the variable immunoglobulin domains of the heavy and light chain each providing three hypervariable loops, which are varied to generate diversity. The recent identification of a novel class of antibody in humans from malaria endemic regions of Africa was therefore surprising as one hypervariable loop contains the entire collagen-binding domain of human LAIR1. Here, we present the structure of the Fab fragment of such an antibody. We show that its antigen-binding site has adopted an architecture that positions LAIR1, while itself being occluded. This therefore represents a novel means of antigen recognition, in which the Fab fragment of an antibody acts as an adaptor, linking a human protein insert with antigen-binding potential to the constant antibody regions which mediate immune cell recruitment.
Indexed as
Identifiers
What OpenQuestion holds
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.