Proteomics

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Analysis of Escherichia coli CyDisCo proteome changes in response to the expression of scFv and the misfolded scFv

ABSTRACT: E. coli CyDisCo strain enables a high yield secretion of disulfide bond-containing proteins to the periplasm via Twin-arginine (Tat) pathway. Introducing two exogenous oxidases: the yeast sulfydryl oxidase (Erv1p) and human protein disulfide isomerase (PDI), the CyDisCo strain changes the cytoplasm into an oxidized environment, where the disulfide bonds can efficiently be formed. In this study, we analyzed the proteome changes upon the expression of disulfide bond-containing scFv and the misfolded scFv in the CyDisCo strain. The correctly folded protein is secreted to the periplasm, while the misfolded protein accumulates exclusively in the inclusion body fraction. We observed a high number of significant changes mostly in proteins associated with protein folding and degradation, oxidative stress, membrane transport and integrity.

INSTRUMENT(S): Synapt MS, LTQ Orbitrap Elite

ORGANISM(S): Escherichia Coli

SUBMITTER: Katarzyna Dolata  

LAB HEAD: Katarzyna Dolata

PROVIDER: PXD010078 | Pride | 2019-02-18

REPOSITORIES: Pride

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Comparative proteome analysis in an Escherichia coli CyDisCo strain identifies stress responses related to protein production, oxidative stress and accumulation of misfolded protein.

Guerrero Montero Isabel I   Dolata Katarzyna Magdalena KM   Schlüter Rabea R   Malherbe Gilles G   Sievers Susanne S   Zühlke Daniela D   Sura Thomas T   Dave Emma E   Riedel Katharina K   Robinson Colin C  

Microbial cell factories 20190129 1

<h4>Background</h4>The Twin-arginine translocation (Tat) pathway of Escherichia coli has great potential for the export of biopharmaceuticals to the periplasm due to its ability to transport folded proteins, and its proofreading mechanism that allows correctly folded proteins to translocate. Coupling the Tat-dependent protein secretion with the formation of disulfide bonds in the cytoplasm of E. coli CyDisCo provides a powerful platform for the production of industrially challenging proteins. In  ...[more]

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