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Structure-function analysis of interleukin-5 utilizing mouse/human chimeric molecules.

A N McKenzie1, S C Barry, M Strath

  • 1National Institute for Medical Research, Mill Hill, London, UK.

The EMBO Journal
|May 1, 1991
PubMed
Summary
This summary is machine-generated.

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Interleukin-5 (IL5) activity differs between species due to specific C-terminal residues. Modifying human IL5 with mouse IL5 sequences in this region restores mouse cell activity and receptor binding.

Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Interleukin-5 (IL5) is a glycoprotein crucial for eosinophil production and activation, with species-specific activity.
  • Murine and human IL5 share 70% sequence similarity but exhibit distinct biological functions, particularly on B cells.
  • Human IL5 is significantly less active in mouse cell assays compared to murine IL5.

Purpose of the Study:

  • To investigate the structural basis for species-specific activity of Interleukin-5 (IL5).
  • To identify the specific regions within the IL5 polypeptide responsible for differential activity in mouse and human cells.
  • To elucidate the role of the C-terminal region in IL5 receptor interaction and biological function.

Main Methods:

  • Construction and expression of hybrid Interleukin-5 (IL5) molecules using fragments from human and mouse sequences.

Related Experiment Videos

  • Assays of hybrid IL5 protein activity in human (TF-1, bone marrow) and mouse (B13, bone marrow) cell systems.
  • Competition binding assays to assess receptor interaction.

    • Main Results:

    • Hybrid IL5 proteins showed comparable activity to wild-type human and mouse IL5 in human cell assays, indicating domain interchangeability without structural compromise.
    • In mouse cell assays, the C-terminal region of IL5 was identified as critical for biological activity.
    • Modification of only eight residues in the C-terminus of human IL5 to match mouse IL5 sequences restored comparable biological activity and indicated receptor interaction in this region.

    Conclusions:

    • The C-terminal domain of Interleukin-5 (IL5) is the primary determinant of species-specific activity.
    • Specific residues within the C-terminus of IL5 are crucial for receptor binding and subsequent biological function in mouse cells.
    • Targeted modifications in the IL5 C-terminus can alter its species-specific activity, offering insights into protein-receptor interactions.