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Volume 272, Number 35, Issue of August 29, 1997 pp. 22072-22079
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Mapping of the Primary Binding Site of Measles Virus to Its Receptor CD46

(Received for publication, May 7, 1997)

Christian J. Buchholz , Daniel Koller , Patricia Devaux , Christian Mumenthaler , Jürgen Schneider-Schaulies ^§§ , Werner Braun ^¶¶ , Denis Gerlier and Roberto Cattaneo

From the  Institut für Molekularbiologie, Abt.I, Universität Zürich, Hönggerberg, CH-8093 Zürich, Switzerland, the  Immunité et Infections Virales, IVMC, CNRS-UCBI, UMR 5537, 69372 Lyon, Cedex 08, France, the  Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, CH-8093 Zürich, Switzerland, the ^§§ Institut für Virologie und Immunologie, Universität Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany, and the ^¶¶ Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, Texas 77555-1157

The measles virus (MV) hemagglutinin binds to the complement control protein (CCP) CD46 primarily through the two external modules, CCP-I and -II. To define the residues involved in binding, 40 amino acids predicted to be solvent-exposed on the CCP-I-II module surface were changed to either alanine or serine. Altered proteins were expressed on the cell surface, and their abilities to bind purified MV particles, a soluble form of hemagglutinin (sH) and nine CD46-specific antibodies competing to different levels with sH attachment, were measured. All proteins retained, at least in part, MV and sH binding, but some completely lost binding to certain antibodies. Amino acids essential for binding of antibodies weakly or moderately competing with sH attachment are situated in the membrane-distal tip of CCP-I, whereas residues involved in binding of strongly sH competing antibodies cluster in the center of CCP-I (Arg-25, Asp-27) or in CCP-II (Arg-69, Asp-70). Both clusters face the same side of CCP-I-II and map close to amino acid exchanges impairing sH binding (E11A, R29A, P39A, and D70A) or MV binding (D70A and E84A) and to a six-amino acid loop, previously shown to be necessary for sH binding.

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