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Related Experiment Videos

Divalent cations affect chain mobility and aggregate structure of lipopolysaccharide from Salmonella minnesota

Patrick Garidel1, Michael Rappolt, Andra B Schromm

  • 1Martin-Luther-Universität Halle, Wittenberg, Institut für Physikalische Chemie, Mühlpforte 1, D-06108 Halle, Germany.

Biochimica Et Biophysica Acta
|September 3, 2005
PubMed
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Divalent cations significantly alter the physicochemical properties and reduce the biological activity of lipopolysaccharide Re (LPS Re). This is primarily due to changes in aggregate structure and lipid A acyl chain mobility, impacting interactions with binding proteins.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Immunology

Background:

  • Lipopolysaccharide Re (LPS Re) is a key component of Gram-negative bacteria.
  • Divalent cations (e.g., Mg2+, Ca2+, Ba2+) are known to influence LPS structure and function.
  • Understanding these interactions is crucial for developing LPS-targeted therapeutics.

Purpose of the Study:

  • To investigate the impact of divalent cations on the physicochemical properties of LPS Re.
  • To determine how these changes affect the biological activity of LPS Re.
  • To elucidate the structural basis for altered LPS Re activity in the presence of divalent cations.

Main Methods:

  • Differential scanning calorimetry (DSC) and Fourier-transform infrared spectroscopy (FT-IR) for acyl chain phase behavior.

Related Experiment Videos

  • Synchrotron radiation X-ray diffraction for aggregate structures.
  • Electron density calculations and assessment of LPS-induced interleukin-6 production in human mononuclear cells.

    • Main Results:

    • Divalent cation salt forms of LPS Re showed significant changes in acyl chain mobility and aggregate structures compared to natural or monovalent cation forms.
    • Biological activity, particularly cytokine production, was markedly reduced for Ca2+ and Ba2+ salt forms.
    • Structural changes included conversion from unilamellar/cubic to multilamellar aggregate structures.

    Conclusions:

    • Divalent cations modulate LPS Re physicochemical properties, leading to reduced biological activity.
    • The transition to multilamellar structures and decreased lipid A acyl chain mobility impede binding protein interactions (LBP, CD14).
    • These findings provide insights into LPS-mediated immune responses and potential therapeutic strategies.