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Related Experiment Videos

A serum lectin (mannan-binding protein) has complement-dependent bactericidal activity.

N Kawasaki1, T Kawasaki, I Yamashina

  • 1College of Medical Technology, Faculty of Pharmaceutical Sciences, Kyoto University.

Journal of Biochemistry
|September 1, 1989
PubMed
Summary
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Serum mannan-binding protein (MBP) exhibits bactericidal activity against E. coli by activating complement. This lectin binds to bacterial cell walls, leading to bacterial death and suggesting a role in host defense.

Area of Science:

  • Immunology
  • Microbiology
  • Biochemistry

Background:

  • Serum mannan-binding protein (MBP) is a lectin that recognizes mannose and N-acetylglucosamine.
  • MBP activates the classical complement pathway.
  • MBP has been implicated in host defense mechanisms.

Purpose of the Study:

  • To investigate the bactericidal activity of serum mannan-binding protein (MBP) against rough strains of Escherichia coli.
  • To elucidate the mechanism of MBP-mediated bacterial killing.
  • To determine the binding characteristics of MBP to E. coli.

Main Methods:

  • Bactericidal assays using purified human serum MBP and guinea pig complement.
  • Measurement of bacterial colony-forming ability.
  • Scatchard plot analysis for MBP binding kinetics.

Related Experiment Videos

  • Inhibition assays with various carbohydrates.

    • Main Results:

    • MBP demonstrated complement-dependent bactericidal activity against E. coli K-12 and B.
    • The bactericidal effect was dependent on MBP and complement concentrations and proceeded via the classical pathway (C4-dependent).
    • MBP binding to E. coli showed a dissociation constant (Kd) of 6 x 10(-9) M and a maximum binding capacity of 30,000 molecules per cell.
    • MBP recognized specific sugars in the E. coli core oligosaccharide, including N-acetylglucosamine and L-glycero-D-manno-heptose.

    Conclusions:

    • Serum mannan-binding protein (MBP) possesses direct bactericidal activity against E. coli through complement activation.
    • MBP binding to E. coli involves recognition of specific carbohydrate structures in the bacterial cell wall.
    • These findings highlight the role of MBP as a crucial component of the innate immune system in combating bacterial infections.