Abstract
A single-chain antibody fragment has been constructed for an antibody that binds to theChlamydia specific carbohydrate structure of the lipopolysaccharide. Single-chain protein was expressed and secreted into the periplasmic space ofE. coli as a fusion protein with the maltose binding protein. The fusion protein was purified in one step by virtue of its ability to bind to maltose. In a sandwich ELISA, the eluted protein boundChlamydia lipopolysaccharide, which demonstrates that the single-chain protein domain will function as part of a fusion protein. The expression of maltose binding fusion proteins into the periplasmic space could be used for production of other single-chain antibodies or protein fragments requiring appropriate folding and disulfide bond formation.
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Malinowski, D.P., Gourley, M., Edelstein, S. et al. Expression of aChlamydia anticarbohydrate single-chain antibody as a maltose binding fusion protein. Cell Biophysics 21, 1–12 (1992). https://doi.org/10.1007/BF02789473
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DOI: https://doi.org/10.1007/BF02789473