TY - JOUR
T1 - Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59
AU - Hahn, William C.
AU - Menu, Elisabeth
AU - Bothwell, Alfred L.M.
AU - Sims, Peter J.
AU - Bierer, Barbara E.
PY - 1992
Y1 - 1992
N2 - The interaction of the T cell glycoprotein CD2 with one ligand, CD58, contributes to T cell function. We have identified CD59, a glycoprotein with complement-inhibitory function, as a second physiological ligand for CD2. Antibodies to CD59 inhibit CD2-dependent T cell activation in murine T cell hybridomas expressing human CD2. In an in vitro binding assay with purified CD58 and CD59, CD2+ cells bind not only immobilized CD58 but also CD59. With two complementary approaches, it was demonstrated that the binding sites on CD2 for CD58 and CD59 are overlapping but nonidentical. These observations suggest that direct interactions between CD2 and both CD58 and CD59 contribute to T cell activation and adhesion.
AB - The interaction of the T cell glycoprotein CD2 with one ligand, CD58, contributes to T cell function. We have identified CD59, a glycoprotein with complement-inhibitory function, as a second physiological ligand for CD2. Antibodies to CD59 inhibit CD2-dependent T cell activation in murine T cell hybridomas expressing human CD2. In an in vitro binding assay with purified CD58 and CD59, CD2+ cells bind not only immobilized CD58 but also CD59. With two complementary approaches, it was demonstrated that the binding sites on CD2 for CD58 and CD59 are overlapping but nonidentical. These observations suggest that direct interactions between CD2 and both CD58 and CD59 contribute to T cell activation and adhesion.
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U2 - 10.1126/science.1377404
DO - 10.1126/science.1377404
M3 - Article
C2 - 1377404
AN - SCOPUS:0026704425
SN - 0036-8075
VL - 256
SP - 1805
EP - 1807
JO - Science
JF - Science
IS - 5065
ER -