Antigenic properties of the coat of Cucumber mosaic virus using monoclonal antibodies

The coat protein (CP) of Cucumber mosaic virus (CMV) was characterized by antigen-capture-ELISA using a panel of monoclonal antibodies (mAbs) which were produced against Pepo-CMV-CP. Comparative analysis of three mAbs with four different strains by competitive ELISA revealed that the binding affinity of the mAb decreased about 10-fold with both MY17- and Y-CMV than with Pepo-CMV. The CP of these three strains showed high homology (∼98%) following comparison in the GenBank database. CMV has a negatively charged loop structure, the βH–βI loop, although the amino acid at position 193 is not conserved. In addition, an amino acid residue identified within the variable region spanning amino acids 191–198, specifically at position 194, showed significant changes in Threonine, Alanine, Alanine, and Lysine of the Pepo-, MY17-, Y-, and M2-CMV strains, respectively. Evidence from competitive ELISA and GenBank database amino acid residues, when taken together, provide strong support suggesting that the dominant epitope site of CMV-CP-specific mAbs is the βH–βI loop 191–198. The four mAbs were chosen because they represent distinct, overlapping epitopes within the group-specific determinant located on the CMV-CP and because they all recognize linear epitopes. Knowledge of specific immunoglobulin genes for a common epitope may lead to insight on pathogen–host co-evolution and may help prevent virus infection in plants.