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Complement Factor H Binds to Human Serum Apolipoprotein E and Mediates Complement Regulation on High Density

Karita Haapasalo1, Kok van Kessel2, Eija Nissilä3

  • 1From the Department of Bacteriology and Immunology, Haartman Institute, and Research Programs Unit, Immunobiology, University of Helsinki, FIN-00014 Helsinki, Finland, Medical Microbiology, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands, K.J.Haapasalo-Tuomainen@umcutrecht.nl.

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Factor H (FH) domains 5-7 (FH5-7) unexpectedly inhibit complement regulation on HDL particles, enhancing microbial phagocytosis. This interaction with apolipoprotein E (apoE) reveals a novel immune evasion mechanism.

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Area of Science:

  • Immunology
  • Complement System Biology
  • Innate Immunity

Background:

  • The alternative complement pathway is crucial for innate immunity but requires regulation by Factor H (FH) to prevent host cell damage.
  • Mutations in FH domains 19-20 and 5-7 are linked to diseases, and these regions bind microbial pathogens for immune evasion.
  • Previous work showed FH5-7 inhibits survival of FH-binding pathogens by blocking FH binding.

Purpose of the Study:

  • To investigate the broader effects of FH5-7 on microbial survival in blood.
  • To elucidate the mechanism by which FH5-7 affects complement regulation and microbial clearance.
  • To identify novel interactions of FH5-7 within plasma components.

Main Methods:

  • Exposure of microbes to FH5-7 in human whole blood.
  • Assessment of microbial survival and neutrophil phagocytosis.
  • Affinity chromatography and mass spectrometry to identify FH-interacting proteins.
  • Analysis of FH5-7 binding to HDL particles in relation to apoE concentration.

Main Results:

  • FH5-7 reduced the survival of both FH-binding and non-FH-binding microbes.
  • This effect was mediated by impaired complement regulation on HDL particles, leading to enhanced neutrophil phagocytosis.
  • FH was found to interact with apolipoprotein E (apoE) via its FH5-7 domains.
  • FH5-7 binding to HDL was dependent on the apoE concentration on the particles.

Conclusions:

  • FH interacts with apoE through its FH5-7 domains.
  • FH5-7 regulates alternative complement pathway activation on plasma HDL particles.
  • This interaction provides a new understanding of microbial immune evasion strategies and complement regulation.