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J Biol Chem, Vol. 275, Issue 14, 10235-10246, April 7, 2000

The Membrane Anchor Influences Ligand Binding Two-dimensional Kinetic Rates and Three-dimensional Affinity of Fcgamma RIII (CD16)*

Scott E. CheslaDagger §, Ping LiDagger , Shanmugam Nagarajan, Periasamy Selvaraj, and Cheng ZhuDagger ||

From the Dagger  George W. Woodruff School of Mechanical Engineering and Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332-0363 and  Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, Georgia 30322

Kinetic rates and affinity are essential determinants for biological processes that involve receptor-ligand binding. By using a micropipette method, we measured the kinetics of human Fcgamma receptor III (CD16) interacting with IgG when the two molecules were bound to apposing cellular membranes. CD16 is one of only four eukaryotic receptors known to exist natively in both the transmembrane (TM, CD16a) and glycosylphosphatidylinositol (GPI, CD16b) isoforms. The biological significance of this anchor isoform coexistence is not clear. Here we showed that the anchor influenced kinetic rates; compared with CD16a-TM, CD16a-GPI bound faster and with higher affinities to human and rabbit IgGs but slower and with lower affinity to murine IgG2a. The same differential affinity patterns were observed using soluble IgG ligands. A monoclonal antibody bound CD16a-GPI with higher affinity than CD16a-TM, whereas another monoclonal antibody reacted strongly with CD16a-TM but weakly with CD16a-GPI. No major differential glycosylation between the two CD16a isoforms was detected by SDS-polyacrylamide gel electrophoresis analysis. We suggest a conformational difference as the mechanism underlying the observed anchor effect, as it cannot be explained by the differing diffusivity, flexibility, orientation, height, distribution, or clustering of the two molecules on the cell membrane. These data demonstrate that a covalent modification of an Ig superfamily receptor at the carboxyl terminus of the ectodomain can have an impact on ligand binding kinetics.

* This work was supported in part by National Science Foundation Grant BCS 9350370, National Institutes of Health Grant AI38282 (to C. Z.), and National Institutes of Health Grant AI30631 (to P. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported in part by National Institutes of Health Training Grant GM08433.

|| To whom correspondence should be addressed: George W. Woodruff School of Mechanical Engineering and Dept. of Biomedical Engineering, Georgia Institute of Technology, Atlanta, GA 30332-0363. Tel.: 404-894-3269; Fax: 404-894-2291; E-mail: cheng.zhu@me.gatech.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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