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(Received for publication, May 7, 1997)
From the 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.
Volume 272, Number 35,
Issue of August 29, 1997
pp. 22072-22079
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
and
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
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