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Related Experiment Videos

Rat mannose-binding protein a binds CD14.

H Chiba1, H Sano, D Iwaki

  • 1Department of Biochemistry, Sapporo Medical University School of Medicine, Chuo-ku, Sapporo 060-8556, Japan.

Infection and Immunity
|February 17, 2001
PubMed
Summary

Mannose-binding protein (MBP) binds to CD14, a receptor for lipopolysaccharide (LPS). This interaction differs from MBP

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Lipopolysaccharide (LPS) triggers inflammation via the CD14 receptor.
  • Collectins, including Mannose-binding protein (MBP), surfactant protein A (SP-A), and SP-D, are involved in innate immunity.
  • SP-A and SP-D have been shown to interact with CD14, modulating LPS responses.

Purpose of the Study:

  • To investigate if Mannose-binding protein (MBP), a collectin homologous to SP-A and SP-D, binds to CD14.
  • To characterize the binding interaction between MBP and CD14.
  • To compare the binding mechanisms of MBP to CD14 and LPS.

Main Methods:

  • Recombinant rat MBP-A and human soluble CD14 were used for binding assays.
  • Binding was assessed in the presence and absence of mannose and EDTA.

Related Experiment Videos

  • Deglycosylated CD14 was used to determine the binding site of MBP-A.
  • MBP-A binding to various forms of LPS (lipid A, rough, and smooth) was compared to CD14 binding.

    • Main Results:

    • Recombinant MBP-A demonstrated concentration-dependent binding to soluble CD14.
    • MBP-A binding to CD14 was unaffected by mannose or EDTA and occurred with deglycosylated CD14, indicating peptide-mediated interaction.
    • MBP-A bound to lipid A and rough LPS but not smooth LPS.
    • EDTA and mannose inhibited MBP-A binding to rough LPS, unlike its binding to CD14.

    Conclusions:

    • CD14 represents a novel ligand for Mannose-binding protein (MBP).
    • MBP-A interacts with the peptide portion of CD14.
    • MBP-A employs distinct recognition mechanisms for CD14 and LPS binding.