• Title of article

    Heterologous Expression of Human IL-29 (IFN-λ1) in Iranian Lizard Leishmania

  • Author/Authors

    -، - نويسنده Biotechnology Department, Shahid Beheshti University of Medical Sciences, Tehran, IR Iran Taromchi, Amir Hossein , -، - نويسنده Biotechnology Department, Shahid Beheshti University of Medical Sciences, Tehran, IR Iran Kazemi, Bahram , -، - نويسنده Department of Genetics, Zanjan Branch, Islamic Azad University, Zanjan, IR Iran Mahmazi, Sanaz , -، - نويسنده Biotechnology Department, Shahid Beheshti University of Medical Sciences, Tehran, IR Iran and Cellular and Molecular Biology Research Center, Shahid Beheshti University of Medical Sciences, Tehran, IR Iran Bandehpour, Mojgan

  • Issue Information
    فصلنامه با شماره پیاپی 43 سال 2013
  • Pages
    7
  • From page
    168
  • To page
    174
  • Abstract
    -
  • Abstract
    Background: Interferons with diffrent functions such as antiviral, antiproliferative and immunomodulatory actions are effctivemedications for a number of diseases. One of these new interferons (IFNs) is Interleukin-29 (IL-29) belongs to the family of IFN-λ hasantiviral activity and its potent in accompanying with IFN-α in treatment of HCV infection has been evaluated (clinical trial phase II).Recombinant IL-29 has been previously produced in multiple expression systems but in this study we cloned and expressed this protein inan Iranian Lizard leishmania (I.L.L) for the fist time.Objectives: The Main objective of this research was to evaluate expression of functional human IL-29 in domestic Lizard leishmania as analternative eukaryotic expression system.Materials and Methods: The IL-29 expression cassette was constructed into a pLEXSY vector. The leishmania cells were transfected byelectroporation. After selection of transfectants, the protein expression was evaluated at RNA and protein levels.Results: Expression cassette was successfully transfected to leishmania cells and expression of recombinant IL-29 was proved by RT-PCRand western blotting. Purifid protein showed 20% activity compared to standard protein. Enzymatic removal of N-glycan resulted to theshift of protein mobility on SDS-PAGE.Conclusions: Easy handling and culture of this eukaryotic host and mammalian cell like posttranslational modifiations are the mainadvantages of this expression host, but the expression yield of this protein is very low and it seems to be not economic for large-scaleproduction.
  • Journal title
    Iranian Journal of Biotechnology (IJB)
  • Serial Year
    2013
  • Journal title
    Iranian Journal of Biotechnology (IJB)
  • Record number

    2064937