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TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap.

Andrew C McShan¹, Christine A Devlin², Giora I Morozov¹

¹Center for Computational and Genomic Medicine, Department of Pathology and Laboratory Medicine, The Children's Hospital of Philadelphia, Philadelphia, PA, USA.

Nature Communications

|May 27, 2021

Summary

Chaperones Tapasin and TAP-binding protein related (TAPBPR) stabilize MHC-I molecules and select peptides. Loop mutations affect TAPBPR

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Area of Science:

Immunology
Molecular Biology
Structural Biology

Background:

Tapasin and TAP-binding protein related (TAPBPR) are crucial chaperones for MHC-I peptide loading.
Previous studies provided structural insights but lacked mechanistic detail on peptide selection.
A variable-length loop was hypothesized to stabilize empty MHC-I molecules.

Purpose of the Study:

To elucidate the molecular mechanism of Tapasin/TAPBPR in MHC-I chaperoning and peptide editing.
To investigate the role of the variable loop in chaperone function.
To understand how TAPBPR influences peptide selection affinity.

Main Methods:

Deep mutagenesis in two expression systems.
Solution NMR, Isothermal Titration Calorimetry (ITC), and Fluorescence Polarization (FP) assays.
Biophysical characterization of MHC-I-chaperone interactions.

Main Results:

Key chaperoning residues are on a scaffolding surface, not the loop.
Loop mutations impact TAPBPR interaction with peptide-loaded MHC-I, affecting editing.
The loop hovers above the groove, promoting peptide capture.
TAPBPR's longer loop facilitates peptide loading in low-ligand environments and stabilizes peptide-MHC-I complexes.

Conclusions:

The loop's position and TAPBPR's longer loop modulate peptide selection and loading efficiency.
This mechanism ensures effective peptide loading and complex stability in diverse cellular conditions.
Findings reveal distinct roles for scaffolding and loop regions in MHC-I chaperone function.