Evidence map›Paper›PMID 32983155›Full record

ReviewFrontiers in immunology2020

Structural Aspects of the Allergen-Antibody Interaction.

Anna Pomés, Geoffrey A Mueller, Maksymilian Chruszcz

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.1field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Human Monoclonal IgE Antibodies-a Major Milestone in Allergy.Current allergy and asthma reports · 2023
    Review
  10. Article
  11. Review
  12. Generation and Characterization of Native and Sialic Acid-Deficient IgE.International journal of molecular sciences · 2022
    Article
  13. The Structural Flexibility of PR-10 Food Allergens.International journal of molecular sciences · 2022
    Article
  14. Article
  15. Allergy, Anaphylaxis, and Nonallergic Hypersensitivity: IgE, Mast Cells, and Beyond.Medical principles and practice : international journal of the Kuwait University, Health Science Centre · 2022
    Review
  16. Article
  17. Review
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 1 country.

Anna PomésIndoor Biotechnologies, Inc., Charlottesville, VA, United States.
Geoffrey A MuellerNational Institute of Environmental Health Sciences, Durham, NC, United States.
Maksymilian ChruszczDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, United States.
Indoor Biotechnologies (United States) · USNational Institute of Environmental Health Sciences · USUniversity of South Carolina · US

Funding

Structural and Functional Characterization of AllergensZIAES102906 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI MUELLER, GEOFFREY · 2010 to 2025
$10.0M
Antigenic determinants of asthma-associated allergens for design of immunotherapy.R01AI077653 · NIAID · INDOOR BIOTECHNOLOGIES · PI MARTIN D. CHAPMAN, Maksymilian Chruszcz · 2009 to 2026
$9.5M
Intramural NIH HHS ZIA ES102906NIAID NIH HHS R01 AI077653
6 · The paper itself

Abstract

The development of allergic disease involves the production of IgE antibodies upon allergen exposure in a process called sensitization. IgE binds to receptors on the surface of mast cells and basophils, and subsequent allergen exposure leads to cross-linking of IgE antibodies and release of cell mediators that cause allergy symptoms. Although this process is quite well-understood, very little is known about the epitopes on the allergen recognized by IgE, despite the importance of the allergen-antibody interaction for the allergic response to occur. This review discusses efforts to analyze allergen-antibody interactions, from the original epitope mapping studies using linear peptides or recombinant allergen fragments, to more sophisticated technologies, such as X-ray crystallography and nuclear magnetic resonance. These state-of-the-art approaches, combined with site-directed mutagenesis, have led to the identification of conformational IgE epitopes. The first structures of an allergen (egg lysozyme) in complex with Fab fragments from IgG antibodies were determined in the 1980s. Since then, IgG has been used as surrogate for IgE, due to the difficulty of obtaining monoclonal IgE antibodies. Technical developments including phage display libraries have contributed to progress in epitope mapping thanks to the isolation of IgE antibody constructs from combinatorial libraries made from peripheral blood mononuclear cells of allergic donors. Most recently, single B cell antibody sequencing and human hybridomas are new breakthrough technologies for finally obtaining human IgE monoclonal antibodies, ideal for epitope mapping. The information on antigenic determinants will facilitate the design of hypoallergens for immunotherapy and the investigation of the fundamental mechanisms of the IgE response.

Indexed as

AllergensAnimalsAntibodiesAntigen-Antibody ComplexAntigen-Antibody ReactionsCrystallography, X-RayEpitope MappingEpitopesHumansImmunoglobulin EMagnetic Resonance SpectroscopyModels, MolecularProtein BindingStructure-Activity RelationshipAllergensAntibodiesAntigen-Antibody ComplexEpitopesImmunoglobulin Eallergenallergycryo-electron microscopyIgE antibodymass spectrometrynuclear magnetic resonancestructureX-ray crystallography

Identifiers

PMID32983155
PMCPMC7492603
OpenAlexW3082605101

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.