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CD2, also known as LFA-2, T11, and the E rosette receptor, is a T lymphocyte surface protein functionally important in adhesion to target cells and T cell triggering. LFA-3 is a widely distributed cell surface protein that functions in adhesion on target cells. We find that LFA-3 is expressed on human E, and that CD2 is a receptor for LFA-3 that mediates T cell adhesion to human E. Pretreatment of T lymphocytes with CD2 mAb or of E with LFA-3 mAb inhibits rosetting. Purified CD2 molecules bind to human E and inhibit rosetting. 125I-CD2 binding to E is inhibited by LFA-3 mAb; reciprocally, binding of LFA-3 mAb to human E is inhibited by pretreatment with purified CD2. Higher concentrations of CD2 aggregate human E; aggregation is inhibited by mAb to LFA-3.

Original publication




Journal article


J Exp Med

Publication Date





664 - 676


Animals, Antibodies, Monoclonal, Antigens, Differentiation, T-Lymphocyte, Antigens, Surface, Binding, Competitive, Bromelains, Cell Adhesion, Cell Line, Erythrocytes, Humans, Lymphocyte Function-Associated Antigen-1, Phytohemagglutinins, Rosette Formation, Sheep, T-Lymphocytes