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Related Concept Videos

Cross-reactivity00:42

Cross-reactivity

Overview
Antigens Involved in Adaptive Immunity01:26

Antigens Involved in Adaptive Immunity

An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Affinity and Avidity01:41

Affinity and Avidity

Overview
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...

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Related Experiment Video

Updated: Jun 1, 2026

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
07:59

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

Published on: March 25, 2014

IgE-binding epitopes: a reappraisal.

R C Aalberse1, R Crameri

  • 1Department of Immunopathology, Sanquin Research and Academic Medical Centre, Amsterdam, the Netherlands. r.aalberse@sanquin.nl

Allergy
|June 1, 2011
PubMed
Summary
This summary is machine-generated.

Understanding immunoglobulin E (IgE) epitopes is complex. While research explores IgE cross-reactivity and epitope clustering, the vast IgE repertoire limits direct clinical applications for allergy diagnosis or prediction.

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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
08:09

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

Related Experiment Videos

Last Updated: Jun 1, 2026

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
07:59

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

Published on: March 25, 2014

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
08:09

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

Area of Science:

  • Immunology
  • Allergen-specific immunotherapy
  • Structural biology

Background:

  • Immunoglobulin E (IgE) plays a central role in allergic reactions.
  • Characterizing IgE epitopes is crucial for understanding allergenicity and developing diagnostics/therapeutics.
  • Current knowledge gaps exist regarding IgE epitope properties and clinical utility.

Purpose of the Study:

  • To review technical aspects and current understanding of IgE epitopes.
  • To explore hypothetical frameworks for IgE epitope data.
  • To assess the clinical relevance of IgE epitope information for patient care and allergenicity prediction.

Main Methods:

  • Analysis of 3D structures of allergen-antibody complexes.
  • Study of allergen analogues and structural mimics.
  • Investigating monoclonal antibodies (mAbs) competing with IgE.
  • Repertoire analysis of cloned IgEs.

Main Results:

  • Limited data suggests IgE may be more cross-reactive than IgG and target 'uninviting' surfaces.
  • Hypotheses include IgE epitope clustering and higher paratope flexibility.
  • IgE epitope repertoire is extensive, potentially limiting direct diagnostic or predictive targeting.

Conclusions:

  • Current evidence suggests the IgE epitope repertoire is too large for specific epitopes to be realistic targets for diagnosis, treatment, or allergenicity prediction.
  • Further research into selected IgE epitope-peptides or mimitopes may offer insights for allergy diagnosis and prognosis, especially for food allergies.
  • The clinical relevance of IgE epitope mapping remains challenging due to repertoire complexity.