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Related Concept Videos

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...
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.
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...

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Related Experiment Video

Updated: May 15, 2026

Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation
12:09

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Published on: February 28, 2019

Studying MHC class II peptide loading and editing in vitro.

AeRyon Kim1, Isabel Ishizuka1, Isamu Hartman1

  • 1Department of Pathology, School of Medicine, Johns Hopkins University, Baltimore, MD, USA.

Methods in Molecular Biology (Clifton, N.J.)
|January 19, 2013
PubMed
Summary

Investigating how human leukocyte antigen (HLA)-DM influences major histocompatibility complex (MHC) class II peptide binding is crucial for understanding immune responses. This study details in vitro methods to quantify these interactions and their kinetics.

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

Published on: March 25, 2014

Related Experiment Videos

Last Updated: May 15, 2026

Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation
12:09

Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation

Published on: February 28, 2019

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

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

Area of Science:

  • Immunology
  • Biochemistry
  • Molecular Biology

Background:

  • Human leukocyte antigen (HLA)-DM plays a key role in selecting immunodominant epitopes.
  • Understanding epitope selection requires examining the biophysical interactions between major histocompatibility complex (MHC) class II molecules, antigenic peptides, and HLA-DM.

Purpose of the Study:

  • To describe in vitro methods for measuring peptide binding to HLA-DR molecules.
  • To investigate the effects of HLA-DM on these peptide-MHC interactions.

Main Methods:

  • Gentle SDS-PAGE Assay for qualitative assessment of peptide-MHC class II complex formation.
  • Fluorescent peptide labeling with G50 spin column separation to measure binding kinetics (association/dissociation rates).
  • BIAcore surface plasmon resonance (SPR) and Intrinsic Tryptophan Fluorescence Assay for real-time kinetic analysis and transient interaction studies.

Main Results:

  • Established methods to qualitatively and quantitatively assess peptide binding to HLA-DR.
  • Demonstrated the ability to measure binding kinetics of peptide-MHC class II complexes.
  • Developed assays to study the influence of HLA-DM on these molecular interactions.

Conclusions:

  • The described in vitro methods provide valuable tools for studying peptide binding to MHC class II molecules.
  • These assays facilitate a deeper understanding of the mechanisms controlling epitope selection influenced by HLA-DM.