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Structure/function of C5 convertases of complement.

N Rawal1, M K Pangburn

  • 1Department of Biochemistry, University of Texas Health Center at Tyler, 11937 US Highway 271, Tyler, TX 75708-3154, USA. nenoo.rawal@uthct.edu

International Immunopharmacology
|May 23, 2001
PubMed
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Complement C3b deposition transforms low-affinity C3/C5 convertases into high-affinity C5 convertases. This enhances C5 cleavage, driving the formation of the cytolytic C5b-9 complex during complement activation.

Area of Science:

  • Immunology
  • Biochemistry
  • Molecular Biology

Background:

  • Complement C3/C5 convertases are key serine proteases in the complement system.
  • Alternative pathway convertases initially cleave C3, leading to C3b deposition.
  • Low-affinity C5 binding by monomeric C3b convertases limits C5 cleavage.

Purpose of the Study:

  • To investigate the mechanism by which C3/C5 convertases transition from low to high affinity for C5.
  • To understand how C3b deposition influences C5 binding and cleavage efficiency.
  • To elucidate the structural basis for high-affinity C5 convertase formation.

Main Methods:

  • Analysis of C3/C5 convertase kinetics and substrate affinity (Km values).
  • Structural studies of C3/C5 convertase complexes.

Related Experiment Videos

  • Indel studies to identify C5 binding sites for the convertase.

    • Main Results:

    • High C3b density on surfaces promotes the formation of C3b complexes with increased affinity for C5.
    • These complexes exhibit Km values for C5 well below physiological concentrations.
    • Structural and indel studies reveal multivalent binding interactions between C3b complexes and C5.
    • This leads to efficient C5 cleavage and production of the C5b-9 complex.

    Conclusions:

    • Increasing C3b deposition converts low-affinity C3/C5 convertases into high-affinity C5 convertases.
    • Multivalent interactions mediated by C3b complexes are crucial for high-affinity C5 binding.
    • This transition is a critical regulatory step in complement-mediated effector functions, including C5b-9 formation.