Use of the human hepcidin gene to build a positive-selection vector for periplasmic expression in Escherichia coli

Jérome Haustant, Annesha Sil, Christopher Maillo-Rius, Agnès Hocquellet, Patricia Costaglioli, Bertrand Garbay, Wilfrid Dieryck (Corresponding Author)

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Recombinant proteins are often produced in the periplasm of Escherichia coli because this facilitates the purification process. The oxidizing environment favors the formation of disulfide bridges. We showed that the periplasmic expression of the human hormone hepcidin 25 (Hep25) fused to the maltose-binding protein (MBP) resulted in cell death. This toxicity was not observed when MBP–Hep25 accumulated in the bacterial cytoplasm, or when Hep25 was addressed to the periplasm without the MBP tag. We then modified the periplasmic expression vector pMALp2E to create pMALp2EH, a positive-selection vector with Hep25 as counterselection gene.
Original languageEnglish
Pages (from-to)35-37
Number of pages3
JournalAnalytical Biochemistry
Volume500
Early online date10 Feb 2016
DOIs
Publication statusPublished - 1 May 2016

Keywords

  • positive selection
  • Hepcidin
  • expression vector
  • cloning

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