An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli. |
| |
Authors: | K Takkinen M L Laukkanen D Sizmann K Alfthan T Immonen L Vanne M Kaartinen J K Knowles T T Teeri |
| |
Institution: | VTT Biotechnical Laboratory, Espoo, Finland. |
| |
Abstract: | Single-chain antibodies consist of the variable, antigen-binding domains of antibodies joined to a continuous polypeptide by genetically engineered peptide linkers. We have used the flexible interdomain linker region of a fungal cellulase to link together the variable domains of an anti-2-phenyloxazolone IgG1 and show here that the resulting single-chain antibody is efficiently secreted and released to the culture medium of Escherichia coli. The yield of affinity-purified single-chain antibody is 1-2 mg/l of culture medium and its affinity and stability are comparable to those of the corresponding native IgG. |
| |
Keywords: | |
|