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.