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Unraveling the molecular mechanism governing the tissue specific expression of IFNλR1

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  • Hashaam Akhtar, Atta-Ur-Rahman School of Applied Biosciences, National University of Sciences and Technology Pakistan
  • ,
  • Ole Jensen Hamming
  • ,
  • Syed Umer Jan, University of Balochistan
  • ,
  • Samar Akhtar, Riphah International University
  • ,
  • Ewa Terczynska-Dyla
  • ,
  • Piotr Siupka
  • ,
  • Adeena Shafique, National University of Sciences and Technology Pakistan
  • ,
  • Rune Hartmann
  • Hajra Sadia, National University of Sciences and Technology Pakistan

The functional receptor for type III interferons (IFNs) is a heterodimer of IFNLR1 and IL10R2. IFNLR1 is expressed in a highly tissue specific manner, with epithelial and liver tissue as the prime expressing tissues in humans. However, knowledge about the molecular pathways responsible for regulating the expression of IFNLR1 is yet unknown. In this study, various bioinformatics tools were used to predict the scores of signal peptides of IFNλR1 and IFNαR1, which was considered as an important difference in the expression of both receptors or participation in regulating the IFNLR1 gene. In silico study revealed that the signal peptide of IFNαR1 had more potential than the signal peptide of IFNλR1 but changing the signal peptide of wild type IFNλR1 with the signal peptide of IFNαR1 in wet lab had barely shown any differences. Selective expression of IFNλR1 was considered to be a plus point towards the targeted anti-viral activity of IFNλs but artificial control on its expression will surely make IFNλs a better drug with enhanced activity. The results of this study may help us in contributing some understanding towards the mechanisms involved in the selective expression of IFNLR1 and exceptionalities involved.

Original languageEnglish
JournalPakistan journal of pharmaceutical sciences
Pages (from-to)795-799
Number of pages5
Publication statusPublished - 1 May 2016

    Research areas

  • Expression, IFNLR1, Interferon lambda, Signal peptide, Transcription factor binding sites (TBS)

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