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Multiple conformations of a human interleukin-3 variant

Y Feng1, W F Hood, R W Forgey

  • 1G.D. Searle and Company, St. Louis, Missouri 63198, USA. ygfeng@nick.monsanto.com

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Summary

Proline isomerization in Interleukin-3 (IL-3) causes conformational changes affecting hematopoietic cell activity. Mutating proline residues reduced IL-3

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Interleukin-3 (IL-3) is a cytokine crucial for hematopoietic cell proliferation and differentiation.
  • The hyperactive hIL-3 variant SC-55494 exhibits significant conformational heterogeneity, observable via NMR spectroscopy.
  • Proline cis-trans isomerization is a known mechanism for protein conformational changes.

Purpose of the Study:

  • To investigate if proline cis-trans isomerization underlies the conformational heterogeneity of SC-55494.
  • To assess the impact of prolyl peptide bond configuration on IL-3's biological activity and receptor binding.

Main Methods:

  • Construction and analysis of six proline-to-alanine mutants of SC-55494.
  • High-resolution Nuclear Magnetic Resonance (NMR) spectroscopy to determine conformational states.
  • Cell proliferation assays and receptor binding affinity measurements to evaluate biological activity.

Main Results:

  • Single proline-to-alanine mutations (P30A, P31A, P33A, P37A) retained conformational heterogeneity.
  • Double (P30A/P31A) and quadruple (P30A/P31A/P33A/P37A) mutants showed significantly reduced heterogeneity.
  • All mutants exhibited reduced cell proliferative activity (40-80% of SC-55494).
  • Mutant P37A maintained equivalent binding affinity to the IL-3 receptor alpha-subunit, while others showed decreased affinity.

Conclusions:

  • The conformational heterogeneity of SC-55494 is attributed to cis-trans isomerization of the R29-P30 and/or P30-P31 peptide bonds.
  • The cis configuration of these peptide bonds is critical for optimal IL-3 interaction with its receptor alpha-subunit.
  • Prolyl peptide bond configuration significantly influences IL-3's biological activity and receptor binding.