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Originally published In Press as doi:10.1074/jbc.M909121199 on March 15, 2000

J. Biol. Chem., Vol. 275, Issue 21, 16146-16154, May 26, 2000
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A Molecular Basis for Functional Peptide Mimicry of a Carbohydrate Antigen*

Ping LuoDagger , Gabriela Canziani§, Gina Cunto-AmestyDagger , and Thomas Kieber-EmmonsDagger

From the Departments of Dagger  Pathology and Laboratory Medicine and § Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104

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 Fucalpha (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 Fucalpha (1-3) from the Fucalpha (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.

To whom correspondence should be addressed: Dept. of Pathology and Laboratory Medicine, Rm. 205, John Morgan Bldg., 36th and Hamilton Walk, Philadelphia, PA 19104-6082. E-mail: tom@xray.med.penn.edu.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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