Evidence map›Paper›PMID 38181840›Full record

ReviewThe Journal of allergy and clinical immunology2024

Precision engineering for localization, validation, and modification of allergenic epitopes.

Anna Pomés, Scott A Smith, Maksymilian Chruszcz, Geoffrey A Mueller, Nicole F Brackett, Martin D Chapman

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of allergy and clinical immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

7 citing papers in PubMed, 16 citations in OpenAlex.

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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

6 authors at 4 institutions in 2 countries.

Anna PomésInBio, Charlottesville, Va. Electronic address: apomes@inbio.com.
Scott A SmithVanderbilt University Medical Center, Nashville, Tenn.
Maksymilian ChruszczMichigan State University, East Lansing, Mich.
Geoffrey A MuellerNational Institute of Environmental Health Sciences, Durham, NC.
Nicole F BrackettInBio, Charlottesville, Va.
Martin D ChapmanInBio, Charlottesville, Va.
Gobierno de Chile · CLMichigan State University · USNational Institute of Environmental Health Sciences · USVanderbilt University Medical Center · 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
Comprehensive antigenic mapping of the human anti-peanut IgE antibody responseR01AI155668 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI SMITH, SCOTT ALAN · 2021 to 2025
$4.1M
Generation and characterization of full-length naturally occurring allergen-specific human IgE mAbsR21AI123307 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI SMITH, SCOTT ALAN · 2017 to 2018
$408k
Intramural NIH HHS ZIA ES102906NIAID NIH HHS R01 AI077653NIAID NIH HHS R01 AI155668NIAID NIH HHS R21 AI123307
6 · The paper itself

Abstract

The allergen-IgE interaction is essential for the genesis of allergic responses, yet investigation of the molecular basis of these interactions is in its infancy. Precision engineering has unveiled the molecular features of allergen-antibody interactions at the atomic level. High-resolution technologies, including x-ray crystallography, nuclear magnetic resonance spectroscopy, and cryo-electron microscopy, determine allergen-antibody structures. X-ray crystallography of an allergen-antibody complex localizes in detail amino acid residues and interactions that define the epitope-paratope interface. Multiple structures involving murine IgG mAbs have recently been resolved. The number of amino acids forming the epitope broadly correlates with the epitope area. The production of human IgE mAbs from B cells of allergic subjects is an exciting recent development that has for the first time enabled an actual IgE epitope to be defined. The biologic activity of defined IgE epitopes can be validated in vivo in animal models or by measuring mediator release from engineered basophilic cell lines. Finally, gene-editing approaches using the Clustered Regularly Interspaced Short Palindromic Repeats technology to either remove allergen genes or make targeted epitope engineering at the source are on the horizon. This review presents an overview of the identification and validation of allergenic epitopes by precision engineering.

Indexed as

AllergensPlant ProteinsAmino Acid SequenceAnimalsAntibodies, MonoclonalCryoelectron MicroscopyEpitopesHumansImmunoglobulin EMiceAllergensAntibodies, MonoclonalEpitopesImmunoglobulin EPlant Proteinsallergen engineeringallergenic epitopesAllergensCRISPRIgE monoclonal antibodynuclear magnetic resonancex-ray crystallography

Identifiers

PMID38181840
PMCPMC10939758
OpenAlexW4390561970

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.