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Título

A similar pattern of interaction for different antibodies with a major antigenic site of foot-and-mouth disease virus: Implications for intratypic antigenic variation

Autor Verdaguer, Núria ; Sevilla, Noemí ; Valero, Mari Luz; Stuart, David I.; Brocchi, Emiliana; Andreu, David; Giralt, Ernest; Domingo, Esteban; Mateu, Mauricio G.; Fita, Ignacio
Palabras clave nonhuman
foot and mouth disease virus
epitope mapping
controlled study
article
antigenic variation
antigen recognition
antigen binding
antibody combining site
priority journal
epitope
virus antigen
virus antibody
Fecha de publicación ene-1998
EditorAmerican Society for Microbiology
Citación Journal of Virology 72(1): 739-748 (1998)
ResumenThe 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.
URI http://hdl.handle.net/10261/110096
Identificadoresissn: 0022-538X
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