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The T lymphocyte glycoprotein CD2 binds the cell surface ligand LFA-3
Nature
|March 1, 1987
Summary
CD2, a T lymphocyte surface protein, acts as both an adhesion molecule and a signaling pathway. This study identifies lymphocyte function-associated antigen-3 (LFA-3) as the natural ligand for CD2, mediating lymphoid cell adhesion.
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- CD2 is a crucial T lymphocyte surface glycoprotein involved in cell adhesion and activation.
- Antibodies to CD2 can inhibit T cell responses, including cytotoxic T-lymphocyte (CTL) mediated killing and T helper cell proliferation.
- CD2's dual role as an adhesion and signaling molecule necessitates understanding its natural ligand.
Purpose of the Study:
- To identify the natural ligand of CD2.
- To elucidate the role of CD2-ligand interactions in T cell adhesion and activation.
Main Methods:
- Utilized purified CD2 to investigate its binding properties.
- Assessed the interaction between CD2 and cell-surface antigens on human cells.
- Investigated the role of CD2-LFA-3 interaction in mediating lymphoid cell adhesion.
Main Results:
- CD2 binds with high affinity to lymphocyte function-associated antigen-3 (LFA-3).
- This CD2-LFA-3 interaction mediates the adhesion of lymphoid cells.
- CD2 functions as an adhesion molecule through its interaction with LFA-3.
Conclusions:
- Lymphocyte function-associated antigen-3 (LFA-3) is the natural ligand for CD2.
- The CD2-LFA-3 interaction is critical for T cell adhesion.
- CD2 plays a significant role in immune cell interactions through LFA-3 binding.