Expression of a bispecific dsFv-dsFv' antibody fragment in Escherichia coli |
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Authors: | Schmiedl A Breitling F Dübel S |
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Affiliation: | Universit?t Heidelberg, Institut für Molekulare Genetik, Im Neuenheimer Feld 230, 69120 Heidelberg, Germany. |
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Abstract: | A bispecific disulfide-stabilized Fv antibody fragment (dsFv-dsFv') consisting of two different disulfide-stabilized Fv antibody fragments connected by flexible linker peptides was produced by secretion of three polypeptide chains into the periplasm of Escherichia coli. The dsFv-dsFv' molecules were enriched by immobilized metal affinity chromatography and further purified by anion-exchange chromatography. The recombinant antibody constructs retained the two parental antigen binding specificities and were able to cross-link the two different antigens. The described dsFv-dsFv' design might be of particular value for therapeutic in vivo applications since improved stability is expected to be combined with minimal immunogenicity. |
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