Surface plasmon resonance screening of synthetic peptides mimicking the immunodominant region of C-S8c1 foot-and-mouth disease virus

The main antigenic site (site A) of foot-and-mouth disease virus (FMDV, str ain C-S8c1) may be adequately reproduced by a 15-peptide with the amino aci d sequence H-YTASARGDLAHLTTT-NH2 (A15), corresponding to the residues 136-1 50 of the viral protein VPI. The effect of amino acid substitutions within A15 on its antigenicity towards monoclonal antibodies (MAb) raised against antigenic site A, has been studied by means of BIAcore technology, based on surface plasmon resonance (SPR). Although these antigenicities have previo usly been determined from enzyme-linked immunosorbent assays (ELISA), the S PR-based technique is superior in that it allows a fast and straightforward screening of antigens while simultaneously providing kinetic data of the a ntigen-antibody interaction. With a view to screening fairly large librarie s of individual peptides, we have inverted the typical SPR experiment by im mobilizing the MAb on the sensor surface and using peptides as soluble anal ytes. We report the validation of this approach through the screening of 44 site A peptides, with results generally in good agreement with the relativ e antigenicities previously determined by competition ELISA. (C) 1999 Elsev ier Science Ltd. All rights reserved.