COMPARISON OF ANTIBODIES RAISED AGAINST THE PEPTIDE-10-24 OF CHICKEN RIBOFLAVIN CARRIER PROTEIN (CRCP) BY CLASSICAL AND MULTIPLE ANTIGEN PEPTIDE (MAP) APPROACHES

Riboflavin carrier protein is an essential protein required for the gr owth and development of the embryo and hence for the maintenance of pr egnancy. Our efforts to delineate the antigenic determinants of chicke n riboflavin carrier protein (cRCP) resulted in the identification of a bioneutralization epitope in the region 10-24 of cRCP. The present w ork compares the properties of the antibodies raised against the pepti de epitope by classical and multiple antigen peptide (MAP) system appr oaches. The extent of cross-reaction of the antibodies to the MAP cons truct with the parent protein was found to be significantly less as co mpared to the antibodies raised against the peptide-diphtheria toroid conjugate, Furthermore, the bioneutralizing ability of the antisera to the MAP construct was also found to be very poor, The results suggest that there are serious limitations in the ability of antibodies raise d against MAP constructs to cross-react with the native proteins.