Production and immunogenicity of multiple antigenic peptide (MAP) constructs derived from the S1 glycoprotein of infectious bronchitis virus (IBV).

Abstract

Synthetic peptides were prepared as multiple antigenic peptide (MAP) constructs to the S1 glycoprotein of infectious bronchitis virus (IBV). The MAP system has been used in the production of anti-peptide and anti-protein antibodies. It has an advantage over linking peptides to a highly immunogenic carrier molecule because antibodies are not produced to the MAP core matrix of lysine residues. Two 25-residue peptides were synthesized to the Arkansas serotype and two were synthesized to the Massachusetts serotype of IBV. The peptide sequences correspond to amino acid residues 64 to 88 and to residues 117 to 141 for each of the IBV serotypes. A MAP construct for each peptide was prepared by linking 4 copies of a peptide to the immunogenetically inert core matrix of lysine residues. The MAP constructs were used to immunize specific pathogen free chickens. Anti-peptide ELISA titers and the dot immunobinding assay against the homologous peptide were positive for all of the sera tested whereas the anti-whole virus ELISA titers and virus neutralization titers were negative for all of the sera tested. Hyperimmune sera against whole virus did not cross react with synthetic peptides made to the heterologous virus suggesting a possible role for the MAP constructs in a serotype specific dot blot or ELISA test for IBV.