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Related Concept Videos

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.
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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.
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Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation
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Human TCR-binding affinity is governed by MHC class restriction.

David K Cole1, Nicholas J Pumphrey, Jonathan M Boulter

  • 1Nuffield Department of Clinical Medicine, John Radcliffe Hospital, University of Oxford, Oxford, United Kingdom.

Journal of Immunology (Baltimore, Md. : 1950)
|April 20, 2007
PubMed
Summary

Human T cell receptor (TCR) binding to peptide-MHC (pMHC) interactions were measured using surface plasmon resonance (SPR). Faster on-rates for TCRs binding to pMHC-I, not off-rates, drive differences in binding affinity.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • T cell recognition relies on T cell receptor (TCR) binding to peptide-MHC (pMHC) complexes.
  • Limited surface plasmon resonance (SPR) data exists for human TCR/pMHC interactions, especially for human class II-restricted responses.

Purpose of the Study:

  • To characterize the binding affinity and kinetics of human T cell receptor (TCR) molecules to their cognate peptide-MHC (pMHC) class I and class II complexes.
  • To address the gap in understanding human TCR/pMHC binding by comparing class I and class II restricted interactions.

Main Methods:

  • Produced a panel of soluble human T cell receptor (TCR) molecules targeting disease epitopes.
  • Utilized surface plasmon resonance (SPR) to measure binding affinity (equilibrium constants) and kinetics (on-rates and off-rates) for eight TCR-I/pMHC-I and six TCR-II/pMHC-II interactions.

Main Results:

  • Significant differences in TCR-binding equilibrium constants were observed between pMHC-I and pMHC-II.
  • Faster association rates (on-rates) were found for TCRs binding to pMHC-I compared to pMHC-II.
  • Dissociation rates (off-rates) for all human TCR/pMHC interactions fell within a narrow range, irrespective of MHC class.

Conclusions:

  • Binding equilibrium constants for human TCR/pMHC-I and TCR/pMHC-II interactions are primarily determined by differences in association rates (on-rates).
  • The consistent off-rates across all tested human TCR/pMHC interactions support the hypothesis that binding half-life is a key determinant of T cell activation.