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Originally published In Press as doi:10.1074/jbc.M010427200 on January 29, 2001

J. Biol. Chem., Vol. 276, Issue 16, 13283-13288, April 20, 2001
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Quantifying the Impact of Membrane Microtopology on Effective Two-dimensional Affinity*,

Tom E. WilliamsDagger , 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 the  Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, Georgia 30322

Just as interactions of soluble proteins are affected by the solvent, membrane protein binding is influenced by the surface environment. This is particularly true for adhesion receptors because their function requires tightly apposed membranes. We sought to demonstrate, and further, to quantify the possible scale of this phenomenon by comparing the effective affinity and kinetic rates of an adhesion receptor (CD16b) placed in three distinct environments: red blood cells (RBCs), detached Chinese hamster ovary (CHO) cells, and K562 cells. Effective affinity reflects both the intrinsic receptor-ligand kinetics and the effectiveness of their presentation by the host membranes. Expression of CD16b, a low affinity Fcgamma receptor, was established by either transfection or spontaneous insertion via its glycosylphosphatidylinositol anchor. Binding to IgG-coated RBCs, measured using a micropipette method, indicated a 50-fold increase in effective affinity for receptors on RBCs over CHO and K562 cells, whereas the off rates were similar for all three. Electron microscopy confirmed that specific tight contacts were broad in RBC-RBC conjugates but sparse in CHO-RBC conjugates. We suggest that through modulation of surface roughness the cytoskeleton can greatly impact the effectiveness of adhesion molecules, even those with no cytoplasmic structures. Implications for locomotion and static adhesion are discussed.

* This work was supported in part by National Science Foundation Grants BCS 9210648 (to C. Z.) and BCS 9350370 (to C. Z.) and National Institutes of Health Grants AI38282 (to C. Z.), AI30631 (to P. S.) and GM08433 (to T. E. W.).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.

The on-line version of this article (available at http://www.jbc.org) contains a video.

|| To whom correspondence should be addressed. Tel.: 404-894-3269; Fax: 404-385-1397; E-mail: cheng.zhu@me.gatech.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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