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'''RETRO-INVERSO ANALOGUE OF THE G-H LOOP OF VP1 IN FOOT-AND-MOUTH-DISEASE (FMD) VIRUS, NMR, 10 STRUCTURES''' | '''RETRO-INVERSO ANALOGUE OF THE G-H LOOP OF VP1 IN FOOT-AND-MOUTH-DISEASE (FMD) VIRUS, NMR, 10 STRUCTURES''' | ||
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==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFW OCA]. | |||
==Reference== | ==Reference== | ||
Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide., Petit MC, Benkirane N, Guichard G, Du AP, Marraud M, Cung MT, Briand JP, Muller S, J Biol Chem. 1999 Feb 5;274(6):3686-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9920919 9920919] | Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide., Petit MC, Benkirane N, Guichard G, Du AP, Marraud M, Cung MT, Briand JP, Muller S, J Biol Chem. 1999 Feb 5;274(6):3686-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9920919 9920919] | ||
[[Category: Benkirane, N.]] | [[Category: Benkirane, N.]] | ||
[[Category: Briand, J P.]] | [[Category: Briand, J P.]] | ||
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[[Category: Muller, S.]] | [[Category: Muller, S.]] | ||
[[Category: Petit, M C.]] | [[Category: Petit, M C.]] | ||
[[Category: | [[Category: Antigen]] | ||
[[Category: | [[Category: Capsid]] | ||
[[Category: | [[Category: Fmdv]] | ||
[[Category: | [[Category: Peptidomimetic]] | ||
[[Category: | [[Category: Retro-inverso]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:27:36 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 11:27, 2 May 2008
RETRO-INVERSO ANALOGUE OF THE G-H LOOP OF VP1 IN FOOT-AND-MOUTH-DISEASE (FMD) VIRUS, NMR, 10 STRUCTURES
OverviewOverview
The antigenic activity of a 19-mer peptide corresponding to the major antigenic region of foot-and-mouth disease virus and its retro-enantiomeric analogue was found to be completely abolished when they were tested in a biosensor system in trifluoroethanol. This suggests that the folding pattern, which is alpha-helix in trifluoroethanol (confirmed by CD measurement), does not correspond to the biologically relevant conformation(s) recognized by antibodies. The NMR structures of both peptides were thus determined in aqueous solution. These studies showed that the two peptides exhibit similar folding features, particularly in their C termini. This may explain in part the cross-reactive properties of the two peptides in aqueous solution. However, the retro-inverso analogue appears to be more rigid than the parent peptide and contains five atypical beta-turns. This feature may explain why retro-inverso foot-and-mouth disease virus peptides are often better recognized than the parent peptide by anti-virion antibodies.
About this StructureAbout this Structure
Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide., Petit MC, Benkirane N, Guichard G, Du AP, Marraud M, Cung MT, Briand JP, Muller S, J Biol Chem. 1999 Feb 5;274(6):3686-92. PMID:9920919 Page seeded by OCA on Fri May 2 11:27:36 2008