A high proportion of anti-peptide antibodies recognize foot-and-mouth disease virus particles.
Synthetic peptides representing the amino acid sequence 141-160 of the structural protein VP1 of foot-and-mouth disease virus (FMDV) elicit virus-neutralizing antibody. Absorption of anti-peptide sera with purified virus particles removed all detectable virus-binding and neutralizing activity, and reduced the ELISA titres against the homologous peptide by 31-41%. The proportion of anti-peptide antibodies that also recognized virus was unaffected by whether the peptide had been inoculated free, carrier-linked or as part of a fusion protein. The majority of these antibodies reacted with sites composed of residues 142-150. Peptides extended at the amino terminus, into regions shown to be poorly antigenic on the intact virus, induced greater neutralizing responses by increasing the proportion of virus-binding antibodies recognizing region 141-150 from 35% to 70%. However, the total proportion of activity against the longer homologous peptide removed by virus absorption remained within the range 31-41%.
Parry
N R
NR
Wellcome Biotech, Beckenham, Kent, U.K.
Syred
A
A
Rowlands
D J
DJ
Brown
F
F
D000914:Antibodies, Viral / Q000096:biosynthesis*; D000956:Antigens, Viral / Q000276:immunology*; D005537:Aphthovirus / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D007106:Immune Sera / Q000276:immunology; D010446:Peptide Fragments / Q000276:immunology*; D014764:Viral Proteins / Q000276:immunology; D015678:Viral Structural Proteins
D000914:Antibodies, Viral; D000956:Antigens, Viral; D007106:Immune Sera; D010446:Peptide Fragments; D014764:Viral Proteins; D015678:Viral Structural Proteins