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Updated: Aug 11, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Lymphocytic CD43 and CD45 bear sulfate residues potentially implicated in cell to cell interactions
V Giordanengo1, M Limouse, J F Peyron
1Laboratoire de Virologie, Unité INSERM U364, Faculté de Médecine, Nice, France.
Insights
This study reveals that CD43, a key lymphocyte surface molecule, is sulfated in activated human lymphocytes. Protein sulfation levels influence CD43-mediated cell aggregation, highlighting its role in cell interactions.
Area of Science:
- Immunology
- Cell Biology
- Glycobiology
Background:
- CD43 is a significant glycosylated molecule on lymphocyte surfaces involved in activation and cell interactions.
- The precise post-translational modifications and functional roles of CD43, particularly sulfation, require further elucidation.
Purpose of the Study:
- To investigate the sulfation status of CD43 and CD45 in human activated lymphocytes and CEM T cells.
- To determine if cell surface protein sulfation modulates CD43-mediated homotypic aggregation.
Main Methods:
- Utilized 35SO4(2-) incorporation for labeling and visualization of sulfated proteins.
- Analyzed CD43 and CD45 expression and sulfation in activated lymphocytes and CEM T cells.
- Assessed the impact of varying sulfation levels on CD43-mediated homotypic aggregation induced by monoclonal antibodies.
Main Results:
- Demonstrated that CD43 is a sulfated molecule in human activated lymphocytes and CEM T cells.
- Confirmed that CD45, another lymphocyte surface glycoprotein, is also sulfated.
- Showed that the extent of cell surface protein sulfation can modulate CD43-mediated homotypic aggregation.
Conclusions:
- CD43 and CD45 are sulfated glycoproteins on human activated lymphocytes.
- Protein sulfation plays a regulatory role in CD43-mediated homotypic aggregation.
- Sulfation sites on CD43 and CD45 may be critical for regulating cell-cell interactions.
Abstract:
CD43 is a major heavily glycosylated lymphocyte surface molecule. It has been shown to play an important role in lymphocyte activation and cell-cell interactions. Here we demonstrate that in human activated lymphocytes and CEM T cells, CD43 is a sulfated molecule. We also observed that CD45, another lymphocyte surface glycoprotein, is a sulfated molecule. 35SO4(2-) incorporation would thus appear to be an appropriate labeling method for CD43 and CD45 visualization. Moreover, we show that the level of cell surface protein sulfation can modulate CD43-mediated homotypic aggregation induced by CD43 monoclonal antibodies. It is well known that glycoprotein sulfation is required for various recognition phenomena. Since there are numerous potential sulfation sites on CD43 and CD45, these residues could play an important role in regulating cell-cell interactions.
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