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A TIRF Microscopy Technique for Real-time, Simultaneous Imaging of the TCR and its Associated Signaling Proteins

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Published on: March 22, 2012

Structural characterization of the TCR complex by electron microscopy.

Ignacio Arechaga¹, Mahima Swamy, David Abia

¹Departamento de Biología Molecular, Universidad de Cantabria (UC) and Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC (CSIC-UC-IDICAN), c/Herrera Oria s/n, 39011 Santander, Spain.

International Immunology

|November 10, 2010

Summary

This study reveals the first 3D structure of the entire T cell receptor (TCR) complex using electron microscopy. The findings provide insights into TCR signaling mechanisms and complex stoichiometry.

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High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

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Published on: May 16, 2017

Area of Science:

Immunology
Structural Biology
Biochemistry

Background:

T cell receptor (TCR) signaling is crucial for adaptive immunity.
Structural data for the complete TCR complex, essential for understanding signal transduction, remains elusive.
Previous studies characterized individual TCR subunits (TCRα/β, CD3 dimers, CD3ζ) using X-ray crystallography and NMR.

Purpose of the Study:

To determine the three-dimensional structure of the entire T cell receptor (TCR) complex.
To elucidate the arrangement and interactions of TCRα/β and CD3 subunits within the complex.
To propose a model for TCR complex stoichiometry and its implications for signaling.

Main Methods:

Purification of the T cell receptor (TCR) complex from T cells under native conditions.
Application of electron microscopy to generate a high-resolution three-dimensional structure.
Utilizing monoclonal antibodies (mAbs) to determine subunit orientation and interaction models.

Main Results:

A pear-shaped three-dimensional structure of the TCR complex was reconstructed (180 × 120 × 65 Å).
The orientation of TCRα/β and CD3 subunits was determined, enabling the suggestion of interaction models.
The reconstructed TCR complex was larger than anticipated for a standard αβγεδεζζ stoichiometry.

Conclusions:

The study provides the first structural model of the complete TCR complex, offering a foundation for understanding TCR-mediated signaling.
The observed larger-than-expected size suggests potential alternative stoichiometries, possibly involving a second TCRαβ unit.
These findings open new avenues for investigating TCR complex assembly and function in T cell activation.