1BCV

SYNTHETIC PEPTIDE CORRESPONDING TO THE MAJOR IMMUNOGEN SITE OF FMD VIRUS, NMR, 10 STRUCTURES

Summary for 1BCV

• Entry DOI: 10.2210/pdb1bcv/pdb
• NMR Information: BMRB: 4212
• Descriptor: PEPTIDE CORRESPONDING TO THE MAJOR IMMUNOGEN SITE OF FMD VIRUS (1 entity in total)
• Functional Keywords: synthetic peptide, antigene
• Cellular location: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 2C: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3A: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3B-1: Virion . Protein 3B-2: Virion . Protein 3B-3: Virion . Picornain 3C: Host cytoplasm . RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : P03308
• Total number of polymer chains: 1
• Total formula weight: 1972.23

Authors

Petit, M.C.,Benkirane, N.,Guichard, G.,Phan Chan Du, A.,Cung, M.T.,Briand, J.P.,Muller, S. (deposition date: 1998-05-03, release date: 1998-11-25, Last modification date: 2024-10-16)

Primary citation

Petit, M.C.,Benkirane, N.,Guichard, G.,Du, A.P.,Marraud, M.,Cung, M.T.,Briand, J.P.,Muller, S.
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.
J.Biol.Chem., 274:3686-3692, 1999

PubMed Abstract: 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.

PubMed: 9920919
DOI: 10.1074/jbc.274.6.3686

Experimental method

SOLUTION NMR