| Summary: | <p>Abstract</p> <p>Background</p> <p><it>Escherichia coli </it>as a frequently utilized host organism for recombinant protein production offers different cellular locations with distinct qualities. The periplasmic space is often favored for the production of complex proteins due to enhanced disulfide bond formation, increased target product stability and simplified downstream processing. To direct proteins to the periplasmic space rather small proteinaceus tags that can be used for affinity purification would be advantageous.</p> <p>Results</p> <p>We discovered that domain D of the <it>Staphylococcus aureus </it>protein A was sufficient for the secretion of various target proteins into the periplasmic space of <it>E. coli</it>. Our experiments indicated the Sec pathway as the mode of secretion, although N-terminal processing was not observed. Furthermore, the solubility of recombinant fusion proteins was improved for proteins prone to aggregation.</p> <p>The tag allowed a straightforward affinity purification of recombinant fusion protein via an IgG column, which was exemplified for the target protein human superoxide dismutase 1 (SOD).</p> <p>Conclusions</p> <p>In this work we present a new secretion tag that combines several advantages for the production of recombinant proteins in <it>E. coli</it>. Domain D of <it>S. aureus </it>protein A protects the protein of interest against N-terminal degradation, increases target protein solubility and enables a straight-forward purification of the recombinant protein using of IgG columns.</p>
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