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T Cell Activation and Clonal Selection

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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.
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Related Experiment Video

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

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Published on: February 28, 2019

Regulation of CD1 antigen-presenting complex stability.

Artur N Odyniec¹, Duarte C Barral, Salil Garg

¹Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.

The Journal of Biological Chemistry

|February 6, 2010

Summary

CD1 heavy chain (HC).beta(2)-microglobulin (beta(2)m) complex stability depends on pH. Lipid antigen binding stabilizes these complexes at neutral cell surface pH, crucial for immune response.

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Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation

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Published on: August 21, 2017

Area of Science:

Immunology
Molecular Biology
Cell Biology

Background:

Major histocompatibility complex (MHC) class I and II molecules rely on peptide antigen binding for assembly, trafficking, and quality control.
The role of lipid antigen binding in the stabilization and quality control of CD1 heavy chain (HC).beta(2)-microglobulin (beta(2)m) complexes remains largely uncharacterized.

Purpose of the Study:

To investigate the impact of lipid antigen binding on the stability and quality control of CD1 HC.beta(2)m complexes.
To elucidate the pH-dependent stability of CD1 complexes and their trafficking through different cellular compartments.

Main Methods:

Analysis of CD1 HC.beta(2)m complex stability across a range of pH conditions.
Assessment of complex stability in the presence and absence of specific lipid antigens.

Main Results:

CD1 HC.beta(2)m complex stability is dictated by distinct pH optima that correlate with their intracellular compartment residence.
While stable at acidic endosomal pH, CD1 complexes require specific lipid antigen binding for stability at neutral cell surface pH (7.4).

Conclusions:

A novel quality control mechanism for CD1 proteins is proposed, involving lipid exchange at low endosomal pH without complex dissociation.
Lipid antigen loading at acidic pH leads to stabilization of the CD1 HC.beta(2)m complex at the neutral pH of the cell surface.