A major antigenic site (site A) of foot-and-mouth disease virus includes multiple overlapping epitopes located within the flexible G-H loop of capsid protein VP1. We have studied the antigenicity of several recombinant E. coli ß-galactosidases displaying the site A from a serotype C virus in different surface regions of the bacterial enzyme. In each one of the explored insertion sites, the recombinant peptide shows different specificity with a set of anti-virus monoclonal antibodies directed to site A. In some of them, the inserted stretch mimics better than free or haemocyanin-coupled peptide the antigenicity of site A in the intact virus. In particular, an insertion within an exposed loop involved in the activating interface of ß-galactosidase (amino acids 272 to 287) led to a significant improvement of the overall reactivity. Since insertions at this site renders proteins enzymatically active, the activating interface could be an adequate place for the presentation of foreign antigens in correctly assembled ß-galactosidase tetramers. These results also suggest that anti-virus antibodies directed against the major antigenic site of FMDV recognize different conformations of the G-H loop, which are better reproduced in some of the recombinant proteins because of the dissimilar restrictions imposed by each particular insertion site. © 1995, Nature Publishing Group. All rights reserved.
|Publication status||Published - 1 Jan 1995|