Modified penicillin acylase signal peptide allows the periplasmic production of soluble human interferon-γ but not of soluble human interleukin-2 by the Tat pathway in Escherichia coli

E. Medina-Rivero, V. E. Balderas-Hernández, L. G. Ordoñez-Acevedo, L. M.T. Paz-Maldonado, A. P. Barba-De La Rosa, A. De León-Rodríguez

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8 Scopus citations

Abstract

Production of periplasmic human interferon-γ (hINF-γ) and human interleukin-2 (hIL-2) by the Tat translocation pathway in Escherichia coli BL21-SI was evaluated. The expression was obtained using the pEMR vector which contains the Tat-dependent modified penicillin acylase signal peptide (mSPpac) driven by the T7 promoter. The mSPpac-hINF-γ was processed and the protein was transported to periplasm. Up to 30.1% of hINF-γ was found in the periplasmic soluble fraction, whereas only 15% of the mSPpac-hIL-2 was processed, but hIL-2 was not found in the periplasmic soluble fraction.

Original languageEnglish
Pages (from-to)1369-1374
Number of pages6
JournalBiotechnology Letters
Volume29
Issue number9
DOIs
StatePublished - Sep 2007
Externally publishedYes

Keywords

  • Periplasm
  • Signal peptide
  • Tat pathway
  • Therapeutic protein

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