Analysis of antibody response to synthetic peptides derived from the fusion protein of measles virus

Citation
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
Citations number
23
Categorie Soggetti
Microbiology
Journal title
MICROBIOLOGICA
ISSN journal
11217138 → ACNP
Volume
22
Issue
1
Year of publication
1999
Pages
19 - 25
Database
ISI
SICI code
1121-7138(199901)22:1<19:AOARTS>2.0.ZU;2-R
Abstract
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.