M. Meqdam et A. Mostratos, Analysis of antibody response to synthetic peptides derived from the fusion protein of measles virus, MICROBIOLO, 22(1), 1999, pp. 19-25
A computer program combining of hydrophilicity, flexibility, surface probab
ility, secondary structure and antigenic index parameters of the amino acid
sequence of measles virus (MV) fusion protein was used to select four poss
ible epitopes. Rabbits were immunized with the synthesized peptides conjuga
ted to purified protein derivative using the homobifunctional cross-linker
bis-sulfosuccinimidyl suberate. Immune stimulating complexes were prepared
with the peptides conjugated to the purified protein derivative carrier usi
ng a dialysis method.
All antisera raised in rabbits against the peptide conjugates had a high ti
ter to the homologous peptides and reacted well with denatured MV as tested
by plate ELISA. None of the sera had neutralizing antibody. Human sera pos
itive for MV antibody reacted strongly with the synthesized peptides indica
ting that the selected locations function as partial antigenic sites. Antis
era against peptide conjugates reacted weakly in immunofluorescence and non
e of these antisera reacted with purified MV proteins in Western blot.
The results obtained in this study indicated that although the computer pro
gram could not predict epitopes important for the neutralization of the MV,
the predicted epitopes are useful for detecting antibodies against MV.