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Originally published In Press as doi:10.1074/jbc.M104364200 on October 25, 2001

J. Biol. Chem., Vol. 277, Issue 3, 2059-2064, January 18, 2002
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Structure of an Anti-blood Group A Fv and Improvement of Its Binding Affinity without Loss of Specificity*

Roula ThomasDagger §, Sonia I. PatenaudeDagger §, C. Roger MacKenzie, Rebecca To, Tomoko Hirama, N. Martin Young, and Stephen V. EvansDagger ||

From the Dagger  Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, Ontario K1H 8M5 and the  Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario K1A 0R6, Canada

The specificity of antibody recognition of the ABO blood group trisaccharide antigens has been explored by crystal structure analysis and mutation methods. The crystal structure of the Fv corresponding to the anti-blood group A antibody AC1001 has been determined to 2.2-Å resolution and reveals a binding pocket that is complementary to the blood group A-trisaccharide antigen. The effect of mutating specific residues lining this pocket on binding to the A and B blood group oligosaccharide antigens was investigated through a panel of single point mutations and through a phage library of mutations in complementarity determining region H3. Both approaches gave several mutants with improved affinity for antigen. Surface plasmon resonance indicated up to 8-fold enhancement in affinity for the A-pentasaccharide with no observable binding to the blood group B antigen. This is the first example of single point mutations in a carbohydrate-binding antibody resulting in significant increases in binding affinity without loss of specificity.

* This work is supported by grants from the Bayer/Red Cross R&D fund (to S. V. E. and N. M. Y.) and the Natural Sciences and Engineering Research Council of Canada (to S. V. E.) and by salary support awards from the Canadian Institutes of Health Research (to S. V. E. and S. I. P.).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.

The atomic coordinates and the structure factors (code 1JV5) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

§ These authors contributed equally to this research.

|| To whom correspondence should be addressed. Tel.: 613-562-5800, Ext. 8437; Fax: 613-562-5440; E-mail: evans@uottawa.ca.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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