image: The paradigm of monoclonal antibodies has been the highly specific interaction of one antibody to one antigen (single or mono-specificity). The binding of antigen and antibody is often schematically depicted as a lock-and-key to highlight the intricate and unique surface complementarity between the antibody and antigen. New research by Bostrom et al. challenges this paradigm. It shows that antibodies are capable of dual specificity. One antibody can adapt its surface to accommodate two entirely different protein antigens and function as two antibodies in combination to target two different antigens, hence, two-in-one antibodies. The report also demonstrates a route through which such two-in-one antibodies can be generated on demand by mutations in the antigen-binding CDR regions of a mono-specificity antibody. This image accompanied the report "Variants of the Antibody Herceptin That Interact with HER2 and VEGF at the Antigen Binding Site," by J. Bostrom et. al. appearing in the March 20, 2009 issue of Science. view more
Credit: Image generated by Allison Bruce and Jenny Bostrom, via <i>Science</i>-AAAS