Monoclonal antibodies specific to Cucumber mosaic virus coat protein possess DNA-hydrolyzing activity

Monoclonal antibodies (mAbs) specific to Cucumber mosaic virus coat protein (CMV-CP) were designed from cDNA and deduced amino acid sequences of the light chain genes of 10 out of 14 different hybridoma cell lines. Ten of these mAbs revealed a very restricted germline family VkII, within which gene bd2 has identical amino acid sequences with VlPase and an i41SL 1-2 catalytic antibody light chain, both of which possess peptidase activity. Four out of the 14 mAbs illustrated another germline family VkIA, within which gene bb1.1 had high homology with BV04-01 light chain mAb, which hydrolyses ssDNA. Interestingly, our mAbs showed DNA-hydrolytic activity at an optimum pH of 4-5, which is a typical pattern of autoimmune diseases in which autoantibodies hydrolyze supercoiled plasmid DNA. This is the first evidence ever that CMV-CP could stimulate catalytic antibodies, which have an identical sequence homology with autoantibodies. Furthermore, the CMV-CP-specific mAbs will be important for isolating antibodies specific to the CPs of bacteria. viruses, cancer cells, etc. that could be used for medical therapy. (C) 2008 Elsevier Ltd. All rights reserved.