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Title: A RETRO-INVERSO PEPTIDE CORRESPONDING TO THE GH LOOP OF FOOT-AND-MOUTH DISEASE VIRUS ELICITS HIGH LEVELS OF LONG-LASTING PROTECTIVE NEUTRALIZING ANTIBODIES

Author
item BRIAND, J-P - INST DE BIOLOGIE, FRANCE
item BENKIRANE, N - INST DE BIOLOGIE, FRANCE
item GUICHARD, G - INST DE BIOLOGIE, FRANCE
item NEWMAN, J-F - FORMER PIADC EMPLOYEE
item VAN REGENMORTEL, M-H - INST DE BIOLOGIE, FRANCE
item Brown, Fred
item MULLER, S - INST DE BIOLOGIE, FRANCE

Submitted to: Proceedings of the National Academy of Sciences (PNAS)
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 9/3/1997
Publication Date: N/A
Citation: N/A

Interpretive Summary: Peptides corresponding to the amino acid sequence of the prominent loop region on the surface of FMDV particles are highly immunogenic. By synthesizing them from D-amino acids they are also less vulnerable to enzymatic degradation. These D-peptides elicit higher and longer lasting neutralizing antibody responses in experimental animals and afford protection against challenge infection.

Technical Abstract: Peptides corresponding to the immunodominant loop located at residues 135-158 on capsid protein VP1 of FMDV generally elicit high levels of anti-peptide and virus-neutralizing antibodies. In some instances, however, the level of neutralizing antibodies is low or even negligible, even though the level of anti-peptide antibodies is high. We have shown previously that the antigenic activity of peptide 141-159 of VP1 of a variant of serotype A can be mimicked by a retro-inverso (all-D retro or retroenantio) peptide analogue. This retro-inverso analogue induced greater and longer-lasting antibody titers than did the corresponding L-peptide. We now show that a single inoculation of the retro-inverso analogue elicits high levels of neutralizing antibodies that persist longer than those induced against the corresponding L-peptides and confer substantial protection in guinea pigs challenged with the cognate virus. In view of the high stability to proteases of retro-inverso peptide analogues and their enhanced immunogenicity, these results have practical relevance in designing potential peptide vaccines.