Author
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BENKIRANE, N - INST DE BIOLOGIE, FRANCE |
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GUICHARD, G - INST DE BIOLOGIE, FRANCE |
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BRIAND, J - INST DE BIOLOGIE, FRANCE |
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MULLER, S - INST DE BIOLOGIE, FRANCE |
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Brown, Fred |
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VAN REGENMORTEL, MARC-H - INST DE BIOLOGIE, FRANCE |
Submitted to: Developments in Biological Standardization
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 7/12/1996 Publication Date: N/A Citation: N/A Interpretive Summary: Peptides corresponding to the highly variable loop on the surface of FMDV particles can elicit the formation of type-specific neutralizing antibodies. To improve their stability towards enzymes which hydrolyse proteins, peptides which mimic the structure of the natural peptides have been synthesized using D-amino acids. These peptides have been shown to mimic the biological properties of the natural peptides. Technical Abstract: Two major limitations to the use of peptides as synthetic vaccines are their poor immunogenicity and low antigenic cross-reactivity with the epitopes of virus particles. Recently, it has been shown that retro-inverso peptides corresponding to an immunodominant epitope of FMDV are able to mimic the structure and antigenic activity of natural L-peptides. A series of L- and retro-inverso peptides of the loop 141-159 of the VP1 protein of FMDV has been synthesized. Antibodies to these peptides were produced by injecting rabbits with peptides covalently coupled to small unilamellar liposomes containing monophosphoryl lipid A as adjuvant. The retro-inverso peptides led to higher serum antibody titers which appeared earlier after the start of immunization and lasted longer than those found with L-peptides. Antibodies to retro-inverso peptides cross-reacted strongly with L-peptides and with virus particles, while guinea pig antisera to VP1 protein and virions cross-reacted strongly with the retro-inverso peptides. In view of their increased stability compared to natural L-peptides, retro inverso peptidomimetics have considerable potential as synthetic viral vaccines. |