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J. Biol. Chem., Vol. 275, Issue 21, 16146-16154, May 26, 2000
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From the Departments of Peptides may substitute for carbohydrate antigens
in carbohydrate-specific immunological reactions. Using the recognition properties of an anti-Lewis Y (LeY) antibody, BR55-2, as a model system, we establish a molecular perspective for peptide mimicry by
comparing the three-dimensional basis of BR55-2 binding to LeY with the
binding of the same antibody to peptides. The peptides compete with
LeY, as demonstrated by enzyme-linked immunosorbent assay and Biacore
analysis. The computer program LUDI was used to epitope map the
antibody-combining site, correlating peptide reactivity patterns. This
approach identified amino acids interacting with the same BR55-2
functional residue groups that recognize the Fuc
A Molecular Basis for Functional Peptide Mimicry of a
Carbohydrate Antigen*
,, and¶
Pathology and Laboratory
Medicine and § Medicine, University of Pennsylvania,
Philadelphia, Pennsylvania 19104
(1-3) moiety of
LeY. Molecular modeling indicates that the peptides adopt an extended
turn conformation within the BR55-2 combining site, serving to overlap
the peptides with the LeY spatial position. Peptide binding is
associated with only minor changes in BR55-2, relative to the
BR55-2-LeY complex. Anti-peptide serum distinguishes the Fuc(1-3)
from the Fuc(1-4) linkage, therefore differentiating difucosylated
neolactoseries antigens. These results further confirm that peptides
and carbohydrates can bind to the same antibody-binding site and that
peptides can structurally and functionally mimic salient features of
carbohydrate epitopes.
*
This work was supported by National Institutes of Health
Grant AI45133.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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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