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Structure/function studies with interferon tau: evidence for multiple active sites

C H Pontzer1, T L Ott, F W Bazer

  • 1Department of Microbiology, University of Maryland, College Park 20742.

Journal of Interferon Research
|June 1, 1994
PubMed
Summary
This summary is machine-generated.

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Interferon-tau (IFN-tau), a pregnancy hormone, shows antiviral and antiproliferative effects without toxicity. Specific peptide regions of IFN-tau are key to its unique interactions with the type I interferon receptor.

Area of Science:

  • * Immunology
  • * Molecular Biology
  • * Reproductive Biology

Background:

  • * Interferon-tau (IFN-tau) is a novel type I interferon with pregnancy recognition functions.
  • * Unlike other interferons, IFN-tau exhibits potent antiviral and antiproliferative activities without causing cytotoxicity.
  • * Understanding the structural basis of IFN-tau's unique functions is crucial for its therapeutic potential.

Purpose of the Study:

  • * To delineate the functional domains of ovine IFN-tau (OvIFN-tau) using synthetic peptides.
  • * To investigate the interaction of OvIFN-tau with the type I interferon receptor.
  • * To identify regions responsible for antiviral and antiproliferative activities.

Main Methods:

  • * Synthesis of six overlapping peptides covering the entire OvIFN-tau sequence.

Related Experiment Videos

  • * Inhibition assays to assess the effect of peptides on OvIFN-tau antiviral activity.
  • * Use of antipeptide antisera to confirm specific peptide interactions.
  • * Testing peptide inhibition of bovine and human IFN-alpha activity.

    • Main Results:

    • * Four peptides (aa 1-37, 62-92, 119-150, 139-172) inhibited OvIFN-tau antiviral activity.
    • * Antipeptide antisera confirmed the specificity of these inhibitory regions.
    • * Peptides OvIFN-tau (62-92), (119-150), and (139-172) inhibited IFN-alpha antiviral activity, suggesting a common receptor binding site.
    • * The amino-terminal peptide (1-37) did not inhibit IFN-alpha, indicating unique receptor interactions for IFN-tau.
    • * Antiproliferative activity was localized to the carboxy-terminal region, with peptide (119-150) being most effective.

    Conclusions:

    • * Distinct domains within IFN-tau contribute to its unique biological activities.
    • * The amino terminus interacts with a specific site on the type I IFN receptor, mediating unique IFN-tau functions.
    • * Internal and carboxy-terminal regions likely engage a common type I IFN receptor site.
    • * The carboxy-terminal region is primarily responsible for the antiproliferative effects of IFN-tau.