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Title: IDENTIFICATION OF A NEUTRALIZING DECAPEPTIDE EPITOPE ON FOOT-AND-MOUTH DISEASE VIRUS

Author
item BRIAND, JEAN - INST DE BIOLOGIE, FRANCE
item MULLER, SYLVIANE - INST DE BIOLOGIE, FRANCE
item GUICHARD, GILLES - INST DE BIOLOGIE, FRANCE
item VAN REGENMORTEL, MARC H. - INST DE BIOLOGIE, FRANCE
item NEWMAN, JOHN F. - FORMER PIADC EMPLOYEE
item Brown, Fred

Submitted to: Cold Spring Harbor Press
Publication Type: Book / Chapter
Publication Acceptance Date: 10/1/1997
Publication Date: N/A
Citation: N/A

Interpretive Summary: Previous work on the immune responses in guinea pigs to the peptide corresponding to the imunodominant loop of FMDV had shown that not all the animals elicited a high neutralizing antibody response. By comparing the reactivity of the sera of good and poor responders with overlapping peptides we have found that the response to the C terminal portion of the peptide is correlated with the level of neutralizing antibodies produced.

Technical Abstract: The major immunogenic site of foot-and-mouth disease virus (FMDV) is contained in a disordered loop comprising amino acids 135-158 of capsid protein VP1, located on the surface of the particle (Acharya et al. 1989). Peptides corresponding to this loop generally elicit levels of neutralizing antibodies that are protective against a severe challenge in experimental animals. In some experiments, however, the level of neutralizing antibodies elicited is low, or even negligible, even though high levels of antipeptide antibodies are produced. These observations led us to attempt to define the structural requirements which need to be met to ensure that good neutralizing antibody responses are obtained consistently.