J. Exp. Med.
© The Rockefeller University Press
0022-1007/97/02/393/12 $2.00
Volume 185 February 1997 393-404

CD80 (B7-1) Binds Both CD28 and CTLA-4 with a Low Affinity and Very Fast Kinetics

By P.  Anton van der Merwe,^* Dale L. Bodian,^§ Susan Daenke, Peter Linsley,^§ and Simon J. Davis

From the ^* Medical Research Council Cellular Immunology Unit, Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom;  Laboratory of Molecular Biophysics, University of Oxford, Oxford OX1 3QU, United Kingdom; ^§ Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, Washington 98121;  Molecular Sciences Division, Nuffield Department of Clinical Medicine, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom

The structurally related T cell surface molecules CD28 and CTLA-4 interact with cell surface ligands CD80 (B7-1) and CD86 (B7-2) on antigen-presenting cells (APC) and modulate T cell antigen recognition. Preliminary reports have suggested that CD80 binds CTLA-4 and CD28 with affinities (K_d values ~12 and ~200 nM, respectively) that are high when compared with other molecular interactions that contribute to T cell-APC recognition. In the present study, we use surface plasmon resonance to measure the affinity and kinetics of CD80 binding to CD28 and CTLA-4. At 37°C, soluble recombinant CD80 bound to CTLA-4 and CD28 with K_d values of 0.42 and 4 µM, respectively. Kinetic analysis indicated that these low affinities were the result of very fast dissociation rate constants (k_off); sCD80 dissociated from CD28 and CTLA-4 with k_off values of 1.6 and 0.43 s¹, respectively. Such rapid binding kinetics have also been reported for the T cell adhesion molecule CD2 and may be necessary to accommodate dynamic T cell-APC contacts and to facilitate scanning of APC for antigen.

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