A RETRO-INVERSO PEPTIDE CORRESPONDING TO THE GH LOOP OF FOOT-AND-MOUTH-DISEASE VIRUS ELICITS HIGH-LEVELS OF LONG-LASTING PROTECTIVE NEUTRALIZING ANTIBODIES
Jp. Briand et al., A RETRO-INVERSO PEPTIDE CORRESPONDING TO THE GH LOOP OF FOOT-AND-MOUTH-DISEASE VIRUS ELICITS HIGH-LEVELS OF LONG-LASTING PROTECTIVE NEUTRALIZING ANTIBODIES, Proceedings of the National Academy of Sciences of the United Statesof America, 94(23), 1997, pp. 12545-12550
Peptides corresponding to the immunodominant loop located at residues
135-158 on capsid protein VP1 of foot-and-mouth disease virus (FMDV) g
enerally elicit high levels of anti-peptide and virus-neutralizing ant
ibodies. In some instances, however, the level of neutralizing antibod
ies is low or even negligible, even though the level of anti-peptide a
ntibodies is high, We have shown previously that the antigenic activit
y 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, Th
is 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 neut
ralizing antibodies that persist longer than those induced against the
corresponding L-peptide and confer substantial protection in guinea p
igs challenged with the cognate virus, In view of the high stability t
o proteases of retro-inverso peptide analogues and their enhanced immu
nogenicity, these results have practical relevance in designing potent
ial peptide vaccines.