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Title

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

AuthorsVerdaguer, Núria ; Sevilla, Noemí ; Valero, Mari Luz; Stuart, David I.; Brocchi, Emiliana; Andreu, David; Giralt, Ernest; Domingo, Esteban ; Mateu, Mauricio G. ; Fita, Ignacio
Keywordsnonhuman
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
Issue DateJan-1998
PublisherAmerican Society for Microbiology
CitationJournal of Virology 72(1): 739-748 (1998)
AbstractThe 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.
URIhttp://hdl.handle.net/10261/110096
Identifiersissn: 0022-538X
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