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Related Concept Videos

Antigen Processing Pathways01:31

Antigen Processing Pathways

MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
MHC Class I: Presenting Endogenous...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Antigens Involved in Adaptive Immunity01:26

Antigens Involved in Adaptive Immunity

An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.

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Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay
19:05

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Published on: October 30, 2015

Major histocompatibility complex class I-ERp57-tapasin interactions within the peptide-loading complex.

Susana G Santos1, Elaine C Campbell, Sarah Lynch

  • 1Bute Medical School, University of St. Andrews, Fife KY16 9TS, Scotland, United Kingdom.

The Journal of Biological Chemistry
|April 27, 2007
PubMed
Summary

Researchers discovered a new complex linking MHC class I, ERp57, and tapasin, crucial for CD8(+) T cell presentation. This finding reveals ERp57

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • The peptide-loading complex in the endoplasmic reticulum is essential for presenting peptides to MHC class I molecules for CD8(+) T cell recognition.
  • ERp57 and protein-disulfide isomerase are known oxidoreductases involved in this complex.
  • ERp57 typically forms a disulfide bond with tapasin within the peptide-loading complex.

Purpose of the Study:

  • To investigate the novel interactions and structural organization of the peptide-loading complex.
  • To elucidate the role of ERp57 in the context of MHC class I peptide loading and presentation.
  • To understand how intracellular redox conditions affect the peptide-loading complex.

Main Methods:

  • Characterization of a novel trimeric complex involving MHC class I heavy chain, ERp57, and tapasin.
  • Analysis of the complex's association with the transporter associated with antigen processing (TAP).
  • Site-directed mutagenesis of ERp57 to probe its interaction with MHC class I.

Main Results:

  • A novel trimeric complex of MHC class I heavy chain, ERp57, and tapasin was identified, associated with TAP.
  • This trimeric complex, usually a minor component, increases under altered intracellular oxidizing conditions.
  • Mutation of a key ERp57 cysteine residue confirmed its direct interaction with the MHC class I peptide-binding groove.

Conclusions:

  • ERp57 directly interacts with MHC class I molecules within the peptide-loading complex.
  • ERp57 and protein-disulfide isomerase likely cooperate to regulate MHC class I redox status during antigen presentation.
  • This interaction is critical for optimal peptide loading and subsequent T cell activation.