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Related Experiment Videos

Multivalent ligand binding by serum mannose-binding protein.

R T Lee1, Y Ichikawa, T Kawasaki

  • 1Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218.

Archives of Biochemistry and Biophysics
|November 15, 1992
PubMed
Summary
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Serum mannose-binding protein (MBP) exhibits bactericidal effects by binding carbohydrates. Unlike hepatic lectins, MBP shows limited affinity enhancement with small ligands, possibly due to distinct subunit organization.

Area of Science:

  • Immunology
  • Biochemistry

Background:

  • Mannose-binding protein (MBP) is a serum defense molecule with carbohydrate-dependent bactericidal activity.
  • MBP shares structural similarities in its carbohydrate-recognition domain with mammalian and chicken hepatic lectins.
  • Both MBP and hepatic lectins achieve high ligand affinity through the clustering of terminal sugar residues on macromolecules.

Purpose of the Study:

  • To investigate the ligand-binding properties of serum mannose-binding protein (MBP).
  • To compare the affinity enhancement mechanisms of MBP with those of hepatic lectins.
  • To explore the structural basis for differences in ligand-binding behavior between MBP and hepatic lectins.

Main Methods:

  • Analysis of carbohydrate-dependent binding affinity (KD) of MBP and hepatic lectins.

Related Experiment Videos

  • Comparison of binding affinities for individual monosaccharides versus clustered sugar residues on macromolecules (e.g., bovine serum albumin).
  • Evaluation of affinity enhancement towards small, di-, and trivalent ligands.

    • Main Results:

    • MBP generates high affinity (nM range) by clustering approximately 30 terminal sugar residues, while individual monosaccharides show low affinity (mM range).
    • MBP does not significantly enhance affinity towards small, di-, and trivalent ligands.
    • Hepatic lectins show a 100- to 1000-fold affinity increase for comparable divalent ligands.

    Conclusions:

    • Differences in subunit organization between MBP and hepatic lectins likely explain their distinct ligand-binding behaviors.
    • MBP's binding strategy relies on multivalent interactions with large structures, unlike hepatic lectins' response to smaller multivalent ligands.