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An Engineered T Cell Receptor Variant Realizes the Limits of Functional Binding Modes.

Nishant K Singh¹, Jesus A Alonso¹, Daniel T Harris²

¹Department of Chemistry and Biochemistry and Harper Cancer Research Institute, University of Notre Dame, Notre Dame, Indiana 46556, United States.

|October 19, 2020

Summary

This summary is machine-generated.

Researchers engineered a T cell receptor (TCR) that binds HLA-A2 without a peptide, altering its geometry. This change prevents normal T cell signaling due to steric hindrance at cell interfaces.

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Area of Science:

Immunology
Molecular Biology
Structural Biology

Background:

T cell receptors (TCRs) are crucial for cellular immunity, recognizing peptide-MHC complexes.
Natural TCRs bind to the peptide-MHC surface, requiring structural and chemical compatibility.

Purpose of the Study:

To describe a molecularly evolved TCR variant with altered binding properties.
To investigate the impact of modified TCR binding geometry on T cell signaling.

Main Methods:

Molecular evolution of a TCR variant.
Analysis of TCR binding to HLA-A2.
Assessment of T cell signaling in solution and at cell-cell interfaces.

Main Results:

An engineered TCR variant binds HLA-A2 independently of the presented peptide.
The variant exhibits a perturbed binding geometry, positioning the TCR away from the peptide-binding groove.
This unique geometry results in a lack of T cell signaling, attributed to steric hindrance at the cell interface.

Conclusions:

Receptor binding geometry significantly influences T cell function.
Germline-encoded TCR residues are critical for productive T cell recognition and signaling.