PDBsum entry 1bfw

Viral protein

PDB id: 1bfw

Contents

Protein chain

20 a.a.

PDB id:

1bfw

Name:

Viral protein

Title:

Retro-inverso analogue of the g-h loop of vp1 in foot-and-mouth- disease (fmd) virus, nmr, 10 structures

Structure:

Vp1 protein. Chain: a. Fragment: the major immunogen region, residues 141-159. Engineered: yes. Other_details: retro-inverso peptide corresponding to the major immunogen region of the foot-and-mouth-disease virus capsid

Source:

not given

NMR struc:

10 models

Authors:

M.C.Petit,N.Benkirane,G.Guichard,A.Phan Chan Du,M.T.Cung,J.P.Briand, S.Muller

Key ref:

M.C.Petit et al. (1999). 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. PubMed id: 9920919 DOI: 10.1074/jbc.274.6.3686

Date:

22-May-98 Release date: 13-Jan-99

Protein chain

No UniProt id for this chain

Struc: 20 a.a.

DOI no: 10.1074/jbc.274.6.3686

J Biol Chem 274:3686-3692 (1999)

PubMed id: 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.

M.C.Petit, N.Benkirane, G.Guichard, A.P.Du, M.Marraud, M.T.Cung, J.P.Briand, S.Muller.

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.

Selected figure(s)

Figure 1.
Fig. 1. Antigenic activity of the parent and retro-inverso (RI) peptide in TFE measured using the biosensor instrument BIAcore. The successive steps of the assay and the controls are described under "Materials and Methods." The results reflect the effect of TFE on the antigenicity of peptides. The antibodies used as probes were not in contact with the TFE solution during the test. The peptides tested are described in the figure. The antibodies tested were from guinea pig antisera (diluted 1:50) raised against the L-peptide 141-159 (a) and RI-peptide 141-159 (b) and from rabbit antisera (diluted 1:20) raised against the L-peptide 141-159 (c) and RI-peptide 141-159 (d). The mouse monoclonal antibody 4x11 directed against the parent peptide IRGERA was tested as a control with the L- and retro-inverso peptides IRGERA (e). The results are expressed in RU.

Figure 4.
Fig. 4. Summary of nonambiguous observed connectivities for the parent (a) and retro-inverso peptide (b). For conventional reasons the numbering of residues was maintained in L- and retro-inverso peptides regardless the orientation of the peptide bonds. The strong, medium, or weak intensities of the NOE cross-peaks are indicated by the thickness of the lines.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (1999, 274, 3686-3692) copyright 1999.

Figures were selected by an automated process.