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CD2 is a transmembrane glycoprotein and a member of the immunoglobulin superfamily, found predominantly on the surface of T cells and natural killer (NK) cells[1][2][4]. It functions as both a cell adhesion molecule and a co-stimulatory receptor, critically involved in the formation and organization of the immunological synapse between T cells and antigen-presenting cells, primarily by binding to its ligand LFA-3 (CD58) in humans[1][2][4]. The interaction facilitates close contact and efficient signaling necessary for T-cell activation, proliferation, and immune response modulation[3][4]. CD2 is a diagnostic marker for T and NK cells and is implicated in diseases such as T-cell lymphomas, some autoimmune diseases, and infections. Therapeutically, monoclonal antibodies targeting CD2, such as siplizumab, are under investigation or clinical use for their immunosuppressive and anti-leukemic/lymphoma effects[4]. Safety issues with anti-CD2 therapies include increased infection risk due to T-cell depletion.
Blocking T-cell activation via CD2–ligand (LFA-3/CD58) interaction; Modulation of T-cell costimulation and adhesion
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