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Complement System01:27

Complement System

The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...
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Protein Denaturation

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Protein Folding

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Complement factor H binds to denatured rather than to native pentameric C-reactive protein.

Svetlana Hakobyan1, Claire L Harris, Carmen W van den Berg

  • 1Department of Medical Biochemistry and Immunology and Pharmacology, School of Medicine, Cardiff University, Cardiff CF14 4XN, UK.

The Journal of Biological Chemistry
|September 13, 2008
PubMed
Summary

The study found that factor H does not bind native C-reactive protein, challenging its role in macular degeneration. Binding only occurs when C-reactive protein is denatured, suggesting prior research may be flawed.

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Area of Science:

  • Immunology
  • Complement System
  • Ocular Disease

Background:

  • Factor H (fH) and C-reactive protein (CRP) are key immune proteins.
  • The Y402H polymorphism in factor H is linked to age-related macular degeneration (AMD).
  • Previous studies suggested differential binding of fH variants to CRP underlies this association.

Purpose of the Study:

  • To investigate the interaction between native human factor H variants (Y402 and H402) and native human C-reactive protein.
  • To determine if differential binding explains the association between factor H Y402H polymorphism and AMD.

Main Methods:

  • Fluid-phase and solid-phase binding assays using purified native human fH variants and CRP.
  • CRP was immobilized under various conditions: non-specific adsorption with Ca(2+), Ca(2+)-dependent ligand binding, absence of Ca(2+), and heat denaturation.
  • Binding was assessed for both fH Y402 and fH H402 variants.

Main Results:

  • No binding of fH variants to CRP in the fluid phase at physiological concentrations.
  • No specific binding of fH variants to native CRP immobilized with or without Ca(2+).
  • Both fH variants bound strongly to heat-denatured CRP and CRP immobilized without Ca(2+), indicating binding to denatured CRP.

Conclusions:

  • The previously reported binding of factor H to C-reactive protein is an artifact of CRP denaturation during immobilization.
  • Differential binding of factor H variants to native C-reactive protein does not explain the association with macular degeneration.
  • Re-evaluation of the role of factor H and C-reactive protein interactions in AMD pathogenesis is warranted.