Monoclonal antibodies defined eight epitope clusters on the IBV peplomer protein, with clusters S1-A to S1-E and S2-G showing moderate to strong virus neutralization at titres higher than 2 log10.
Identified eight epitope clusters on the IBV peplomer protein and correlated them with viral neutralization and hemagglutination inhibition.
Monoclonal antibodies (MAbs) directed against structural proteins of infectious bronchitis virus (IBV) were produced to analyse the antigenic structure of this virus. Competitive binding of enzyme-labelled and unlabelled MAbs to IBV peplomer protein was analysed in an antibody binding assay to test the relatedness of the epitopes defined by the MAbs. Based on the competition groups, eight epitope clusters were defined (S-A to S-H); six of these clusters (S1-A to S1-F) were located on the S1 subunit and two (S2-G and S2-H) on the S2 subunit of the peplomer protein. Epitope clusters S1-A and S1-B overlapped extensively. The biological activities of the MAbs were determined and correlated to the epitope clusters. Monoclonal antibodies directed against epitope clusters S1-A to S1-E and one MAb directed against cluster S2-G moderately to strongly neutralized IBV at titres higher than 2 log10, whereas the remaining MAbs, directed against S1 and S2, neutralized at titres lower than 2 log10. One MAb, directed against cluster S1-D, inhibited the agglutination of chicken erythrocytes.
Koch et al. (Sat,) conducted a other in Avian infectious bronchitis virus. Monoclonal antibodies against structural proteins of infectious bronchitis virus was evaluated on Antigenic structure and biological activities of IBV peplomer protein. Monoclonal antibodies defined eight epitope clusters on the IBV peplomer protein, with clusters S1-A to S1-E and S2-G showing moderate to strong virus neutralization at titres higher than 2 log10.
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