Immunoglobulin domain crossover as a generic approach for the production of bispecific IgG antibodies.

@article{Schaefer2011ImmunoglobulinDC,
  title={Immunoglobulin domain crossover as a generic approach for the production of bispecific IgG antibodies.},
  author={Wolfgang Schaefer and Joerg Thomas Regula and Monika B{\"a}hner and J{\"u}rgen Schanzer and Rebecca Croasdale and Harald D{\"u}rr and Christian Gassner and Guy Georges and Hubert Kettenberger and Sabine Imhof-Jung and Manfred Schwaiger and Kay G Stubenrauch and Claudio Sustmann and Matthew Thomas and Werner V. Scheuer and Christian Klein},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 27},
  pages={
          11187-92
        }
}
We describe a generic approach to assemble correctly two heavy and two light chains, derived from two existing antibodies, to form human bivalent bispecific IgG antibodies without use of artificial linkers. Based on the knobs-into-holes technology that enables heterodimerization of the heavy chains, correct association of the light chains and their cognate heavy chains is achieved by exchange of heavy-chain and light-chain domains within the antigen binding fragment (Fab) of one half of the… CONTINUE READING
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