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Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

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Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

Tapasin's protein interactions in the rainbow trout peptide-loading complex.

Lital Sever¹, Nguyen T K Vo¹, Niels C Bols¹

¹Department of Biology, University of Waterloo, 200 University Ave W. Waterloo, Ontario, N2L 3G1, Canada.

Developmental and Comparative Immunology

|December 19, 2017

Summary

Rainbow trout immune cells share key protein interactions with the human peptide loading complex (PLC). A novel tapasin variant may regulate PLC assembly in fish.

Keywords:

Antigen presentation Peptide loading complex Rainbow trout Tapasin

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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

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Published on: December 20, 2017

Area of Science:

Immunology
Molecular Biology
Fish Biology

Background:

Major histocompatibility complex (MHC) class I receptors are crucial for adaptive immunity, presenting peptides to T cells.
The peptide loading complex (PLC) in the endoplasmic reticulum facilitates MHC class I assembly in humans.
The PLC has not been previously characterized in fish.

Purpose of the Study:

To investigate the conservation of protein-protein interactions within the PLC in fish.
To identify components of the PLC in a rainbow trout cell line.
To explore potential novel regulatory mechanisms of PLC assembly in teleosts.

Main Methods:

Co-immunoprecipitation assays were used to identify protein interactions.
Mass spectrometry was employed to analyze protein complexes.
A rainbow trout monocyte/macrophage cell line (RTS11) was utilized.

Main Results:

Protein-protein interactions within the human PLC, including tapasin with transporter associated with antigen processing (TAP), MHC class I, and ERp57, are conserved in rainbow trout.
A 20 kDa tapasin variant associated with ERp57, forming a 75 kDa heterodimer.
This suggests a potential novel alternatively spliced tapasin isoform.

Conclusions:

The core machinery for peptide loading in fish shares similarities with mammals.
A novel tapasin variant may play a regulatory role in teleost peptide loading complex formation.
This finding contributes to understanding fish adaptive immunity and MHC class I assembly.