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Science 26 June 1992:
Vol. 256. no. 5065, pp. 1805 - 1807
DOI: 10.1126/science.1377404
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Articles

Science, Vol 256, Issue 5065, 1805-1807
Copyright © 1992 by American Association for the Advancement of Science

articles

Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59

WC Hahn, E Menu, AL Bothwell, PJ Sims, and BE Bierer

Division of Pediatric Oncology, Dana-Farber Cancer Institute, and Harvard Medical School, Boston, MA.

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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Elimination of Potential Sites of Glycosylation Fails to Abrogate Complement Regulatory Function of Cell Surface CD59.
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The Membrane-proximal Scavenger Receptor Cysteine-rich Domain of CD6 Contains the Activated Leukocyte Cell Adhesion Molecule Binding Site.
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