Ligands

Employing transfection of cells with mutagenized plasmids or human CD2 chimeric and mutant proteins, distinct CD2 epitopes are defined by monoclonal antibodies and mapped to one of the Ig-like domains of the CD2 ectodomain. CD2 binds to the ubiquitously expressed cell surface glycoprotein, CD58, which is present on many human cell types including antigen-presenting cells and endothelial cells. A sheep homolog of CD58 exists which binds to human CD2, providing the molecular explanation for the fortuitous observation that human T lymphocytes and sheep blood cells spontaneously form rosettes. A second structurally related ligand, CD48, binds to CD2 but with an affinity two orders of magnitude weaker than that of the CD2/CD58 interaction. CD59 is also thought to bind to CD2.

Interactions of CD2 with its ligands are mediated through the N-terminal membrane distal Ig-like domain. The precise role of the second or membrane-proximal Ig domain has not been elucidated in depth, although activation of T cells in response to paired mitogenic combinations of CD2-specific monoclonal antibodies requires that one monoclonal antibody is directed against an epitope (CD2R) within or closely related to this region.

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