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J. Biol. Chem., Vol. 275, Issue 28, 21262-21271, July 14, 2000

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Binding of High Density Lipoprotein (HDL) and Discoidal Reconstituted HDL to the HDL Receptor Scavenger Receptor Class B Type I^*
EFFECT OF LIPID ASSOCIATION AND APOA-I MUTATIONS ON RECEPTOR BINDING^*

Kalliopi N. Liadaki^§, Tong Liu^§¶, Shangzhe Xu^§, Brian Y. Ishida^§**, Philippe N. Duchateaux^**, Jonathan P. Krieger, John Kane, Monty Krieger, and Vassilis I. Zannis^¶§§

From the  University of Crete, Department of Biochemistry and Institute of Molecular Biology and Biotechnology, Heraklion, Crete, Greece 71110, the  Biology Department, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, the  Cardiovascular Research Institute, School of Medicine, University of California, San Francisco, California 94143, the ^** Department of Medicine, University of California, San Francisco, California 94143, and the ^¶ Section of Molecular Genetics, Whitaker Cardiovascular Institute, Department of Medicine and Biochemistry, Boston University Medical Center, W-509, Boston, Massachusetts 02118

The binding of apoA-I-containing ligands to the HDL receptor scavenger receptor class B type I (SR-BI) was characterized using two different assays. The first employed conventional binding or competition assays with ¹²⁵I-labeled ligands. The second is a new nonradioactive ligand binding assay, in which the receptor-associated ligand is detected by quantitative immunoblotting ("immunoreceptor assay"). Using both methods, we observed that the K_d value for spherical HDL (density = 1.1-1.13 g/ml) was ~16 µg of protein/ml, while the values for discoidal reconstituted HDL (rHDL) containing proapoA-I or plasma apoA-I were substantially lower (~0.4-5 µg of protein/ml). We also observed reduced affinity and/or competition for spherical ¹²⁵I-HDL cell association by higher relative to lower density HDL and very poor competition by lipid-free apoA-I and pre--1 HDL. Deletion of either 58 carboxyl-terminal or 59 amino-terminal residues from apoA-I, relative to full-length control apoA-I, resulted in little or no change in the affinity of corresponding rHDL particles. However, rHDL particles containing a double mutant lacking both terminal domains competed poorly with spherical ¹²⁵I-HDL for binding to SR-BI. These findings suggest an important role for apoA-I and its conformation/organization within particles in mediating HDL binding to SR-BI and indicate that the NH₂ and COOH termini of apoA-I directly or indirectly contribute independently to binding to SR-BI.

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