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J Virol, January 1998, p. 739-748, Vol. 72, No. 1
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

A Similar Pattern of Interaction for Different Antibodies with a Major Antigenic Site of Foot-and-Mouth Disease Virus: Implications for Intratypic Antigenic Variation

Nuria Verdaguer,1 Noemi Sevilla,2 Mari Luz Valero,3 David Stuart,4 Emiliana Brocchi,5 David Andreu,3 Ernest Giralt,3 Esteban Domingo,2,* Mauricio G. Mateu,2 and Ignasi Fita1

Centre de Investigació i Desenvolupament (CSIC), Jordi Girona 6, 08028 Barcelona,1 Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid,2 and Department de Química Orgànica, Universitat de Barcelona, 08028 Barcelona,3 Spain; Laboratory of Molecular Biophysics, University of Oxford, Oxford OX1 3QU, United Kingdom4; and Istituto Zooprofilattico Sperimentale della Lombardia e dell'Emilia, 25125 Brescia, Italy5

Received 24 March 1997/Accepted 22 September 1997

The three-dimensional structures of the Fab fragment of a neutralizing antibody raised against a foot-and-mouth disease virus (FMDV) of serotype C1, alone and complexed to an antigenic peptide representing the major antigenic site A (G-H loop of VP1), have been determined. As previously seen in a complex of the same antigen with another antibody which recognizes a different epitope within antigenic site A, the receptor recognition motif Arg-Gly-Asp and some residues from an adjacent helix participate directly in the interaction with the complementarity-determining regions of the antibody. Remarkably, the structures of the two antibodies become more similar upon binding the peptide, and both undergo considerable induced fit to accommodate the peptide with a similar array of interactions. Furthermore, the pattern of reactivities of five additional antibodies with versions of the antigenic peptide bearing amino acid replacements suggests a similar pattern of interaction of antibodies raised against widely different antigens of serotype C. The results reinforce the occurrence of a defined antigenic structure at this mobile, exposed antigenic site and imply that intratypic antigenic variation of FMDV of serotype C is due to subtle structural differences that affect antibody recognition while preserving a functional structure for the receptor binding site.

* Corresponding author. Mailing address: Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain. Phone: 34-1-3978485. Fax: 34-1-3974799. E-mail: edomingo{at}cbm.uam.es.




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