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BMC Biotechnol. 2018 May 29;18(1):30. doi: 10.1186/s12896-018-0443-0.

The production of a recombinant tandem single chain fragment variable capable of binding prolamins triggering celiac disease.

Author information

1
Research Division Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, Vienna, Austria.
2
Sciotec Diagnostics Technologies GmbH, Ziegelfeldstr. 3, 3430, Tulln, Austria.
3
Sciotec Diagnostics Technologies GmbH, Ziegelfeldstr. 3, 3430, Tulln, Austria. f.forster@sciotec.at.
4
Research Division Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, Vienna, Austria. oliver.spadiut@tuwien.ac.at.

Abstract

BACKGROUND:

Celiac disease (CD) is one of the most common food-related chronic disorders. It is mediated by the dietary consumption of prolamins, which are storage proteins of different grains. So far, no therapy exists and patients are bound to maintain a lifelong diet to avoid symptoms and long-term complications. To support those patients we developed a tandem single chain Fragment variable (tscFv) acting as a neutralizing agent against prolamins. We recombinantly produced this molecule in E. coli, but mainly obtained misfolded product aggregates, so-called inclusion bodies, independent of the cultivation strategy we applied.

RESULTS:

In this study, we introduce this novel tscFv against CD and present our strategy of obtaining active product from inclusion bodies. The refolded tscFv shows binding capabilities towards all tested CD-triggering grains. Compared to a standard polyclonal anti-PT-gliadin-IgY, the tscFv displays a slightly reduced affinity towards digested gliadin, but an additional affinity towards prolamins of barley.

CONCLUSION:

The high binding specificity of tscFv towards prolamin-containing grains makes this novel molecule a valuable candidate to support patients suffering from CD in the future.

KEYWORDS:

Celiac disease; E. coli; ELISA; Inclusion body; Single chain fragment variable

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