Author
SILIGARD, G - UNIVERSITY OF LONDON | |
DRAKE, A - UNIVERSITY OF LONDON | |
MASCAGNI, P - UNIVERSITY OF LONDON | |
ROWLANDS, D - UNIVERSITY OF LONDON | |
BROWN, FRED - YALE UNIVERSITY | |
GIBBONS, W - LONDON ENGLAND |
Submitted to: European Journal of Biochemistry
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 3/19/1991 Publication Date: N/A Citation: N/A Interpretive Summary: The shape of the part of foot-and-mouth disease virus which confers protection against the disease differs between different isolates of the virus. By determining its shape in several different isolates we have found that even minor changes are sufficient to eliminate cross- protection. Technical Abstract: The conformational features of four related antigenic peptides (A,B,C and USA) from the immunogenic loop region of foot-and-mouth disease virus, assessed by CD, were found to correlate with their serological properties. The CD spectra of the four peptides, obtained under cryogenic and solvent titration conditions, were consistent with three conformational lcomponents (a left-handed extended helix, an x-helix and a 3[10] helix) for peptides A and C and four components (a B-turn of type II, an x-helix, a y-turn and a 3[10] helix) for peptides B and USA. The amino acid substitutions at positions 148 and 153, which distinguish the peptides, are therefore responsible for both their conformational and antigenic differences. |