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Published on: August 1, 2014
Association between GM3 and CD4-Ick complex in human peripheral blood lymphocytes
M Sorice1, T Garofalo, R Misasi
1Dipartimento di Medicina Sperimentale e Patologia, Universitá di Roma La Sapienza, Italy.
Glycoconjugate Journal
|February 24, 2001
Summary
Ganglioside GM3 interacts with CD4 and p56Ick in human lymphocytes, forming complexes in membrane microdomains. This interaction, crucial for cell signaling, does not require p56Ick for GM3-CD4 binding.
Area of Science:
- Immunology
- Cell Biology
- Glycobiology
Background:
- Previous observations suggested molecular interactions involving GM3, CD4, and p56Ick within human peripheral blood lymphocyte (PBL) microdomains.
- Understanding these interactions is key to elucidating mechanisms of lymphocyte activation and signaling.
Purpose of the Study:
- To further investigate the molecular interactions between GM3, CD4, and p56Ick in human PBL microdomains.
- To determine the role of p56Ick in the association between GM3 and CD4.
Main Methods:
- Immunoelectron microscopy for GM3 distribution analysis.
- Scanning confocal microscopy for colocalization studies of GM3 and CD4.
- Co-immunoprecipitation experiments to assess molecular complex formation.
- Analysis in U937 cell line (CD4+, p56Ick-) to evaluate p56Ick-independent interactions.
Main Results:
- GM3 molecules exhibited uneven distribution on the lymphocyte surface, with CD4 molecules localizing to GM3-enriched domains.
- Co-immunoprecipitation confirmed that GM3 binds to the CD4-p56Ick complex in human PBL.
- GM3-CD4 interaction was observed in p56Ick-negative U937 cells, indicating p56Ick is not required for this binding.
Conclusions:
- GM3-enriched microdomains in human PBL contain functional multimolecular complexes involving CD4.
- The interaction between GM3 and CD4 can occur independently of p56Ick.
- These findings suggest a role for GM3-enriched domains in lymphocyte signal transduction and activation.

