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Related Concept Videos

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.
Antigen Processing Pathways01:31

Antigen Processing Pathways

MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
MHC Class I: Presenting Endogenous...
T Cell Activation and Clonal Selection01:22

T Cell Activation and Clonal Selection

T cells are integral to our adaptive immune system, recognizing and effectively responding to foreign antigens. T cell activation and clonal selection are pivotal in orchestrating this immune response. This article elucidates these mechanisms, detailing the roles of cluster of differentiation (CD) markers, major histocompatibility complex (MHC) molecules, costimulatory signals, and the process of clonal selection.
Naive T cells that have not yet encountered an antigen express two primary CD...
Cross-reactivity00:42

Cross-reactivity

Overview

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Related Experiment Video

Updated: Jul 6, 2026

Overlapping Peptide Library to Map Qa-1 Epitopes in a Protein
08:04

Overlapping Peptide Library to Map Qa-1 Epitopes in a Protein

Published on: December 20, 2017

HLA class II DQ epitopes.

Chun-Tsan Deng1, Junchao Cai, Christine Tarsitani

  • 1One Lambda, Inc., Canoga Park, CA, USA.

Clinical Transplants
|March 28, 2008
PubMed
Summary

Researchers identified specific epitopes on DQ molecules using allo- and monoclonal antibodies. They found that DQ molecules have distinct DQB and DQA1 epitopes, with some sites being unique and others having multiple possibilities.

Area of Science:

  • Immunogenetics
  • Molecular immunology
  • Histocompatibility

Background:

  • DQ molecules are heterodimers crucial in immune responses.
  • Understanding DQ epitopes is vital for transplantation and autoimmune disease research.
  • Distinct reaction profiles of antibodies reveal epitope specificities.

Purpose of the Study:

  • To define specific epitopes on human leukocyte antigen (HLA) DQ molecules.
  • To characterize the antibody recognition sites on DQ alpha (DQA) and DQ beta (DQB) chains.
  • To analyze the molecular basis of DQ epitope diversity.

Main Methods:

  • Utilized 17 allosera and 35 DQ-specific monoclonal antibodies.
  • Employed HLA class II single antigen beads coated with purified recombinant DQ molecules.

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Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis
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Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Published on: October 15, 2021

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Last Updated: Jul 6, 2026

Overlapping Peptide Library to Map Qa-1 Epitopes in a Protein
08:04

Overlapping Peptide Library to Map Qa-1 Epitopes in a Protein

Published on: December 20, 2017

Personalized Peptide Arrays for Detection of HLA Alloantibodies in Organ Transplantation
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Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis
09:32

Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Published on: October 15, 2021

  • Analyzed distinct antibody reaction profiles to map epitopes.

    • Main Results:

    • Defined 17 DQ epitopes, 16 correlating to DQB specificities and one to DQA1*0201.
    • Identified 7 DQB epitopes recognized by both allo- and monoclonal antibodies.
    • Found that 10 epitopes involve 1-3 amino acids, while 7 have multiple potential sites.
    • Confirmed epitope amino acid residues are unique to DQ antigens and exposed on the molecule's surface.

    Conclusions:

    • DQ molecules possess distinct DQB and DQA1 epitopes.
    • Epitope mapping reveals molecular details crucial for understanding immune recognition.
    • A single HLA antigen may comprise multiple epitopes, necessitating detailed molecular analysis.