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Related Experiment Video

Updated: May 25, 2026

Visualizing Antigen Specific CD4+ T Cells using MHC Class II Tetramers

Visualizing Antigen Specific CD4+ T Cells using MHC Class II Tetramers

Published on: March 6, 2009

Dynamics within tetraspanin pairs affect MHC class II expression.

Tineke van den Hoorn¹, Petra Paul, Lennert Janssen

¹Division of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.

Journal of Cell Science

|February 4, 2012

Summary

This summary is machine-generated.

Tetraspanins like CD63 within multivesicular bodies (MVBs) influence major histocompatibility complex class II (MHC-II) expression. CD63 stably interacts with MHC-II and controls its expression, unlike CD82.

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Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Published on: October 15, 2021

Area of Science:

Cell Biology
Immunology
Molecular Biology

Background:

Late endosomal multivesicular bodies (MVBs) contain internal vesicles (ILVs) with diverse protein assemblies.
Tetraspanins, including CD63 and CD82, are enriched in ILVs and may interact with major histocompatibility complex class II (MHC-II) and its chaperone human leukocyte antigen (HLA)-DM.

Purpose of the Study:

To investigate the impact of four tetraspanin proteins (CD9, CD63, CD81, CD82) on MHC-II expression in late endosomes.
To elucidate the dynamic interactions between tetraspanins, MHC-II, and HLA-DM within MVB subdomains.

Main Methods:

Gene silencing of CD9, CD63, CD81, and CD82.
Confocal Förster resonance energy transfer (FRET) technology to measure protein-protein interactions.
Analysis of MHC-II expression and peptide loading.

Main Results:

Silencing CD9, CD63, and CD81 increased MHC-II expression, while silencing CD82 had no effect.
Peptide loading remained unaffected by tetraspanin silencing.
CD63 demonstrated stable association with MHC-II, and CD82 with HLA-DM, within MVB subdomains. Interactions between CD63-MHC-II and CD82-HLA-DM varied, while CD63-CD82 interactions were stable.

Conclusions:

CD63, but not CD82, directly and stably interacts with MHC-II within MVB subdomains.
CD63 plays a significant role in controlling MHC-II expression, providing novel insights into tetraspanin-mediated regulation.
This study provides the first visualization of protein dynamics within tetraspanin assemblies in MVB subdomains.