C1q binding and complement activation by prions and amyloids

Robert B. Sim, Uday Kishore, Christian L. Villiers, Patrice N. Marche, Daniel A. Mitchell

Research output: Contribution to journalArticlepeer-review

45 Citations (Scopus)

Abstract

C1q binds to many non-self and altered-self-materials. These include microorganisms, immune complexes, apoptotic and necrotic cells and their breakdown products, and amyloids. C1q binding to amyloid fibrils found as extracellular deposits in tissues, and subsequent complement activation are involved in the pathology of several amyloid diseases, such as Alzheimer's disease. Prion diseases, such as scrapie also involve formation of amyloid by polymerization of the host prion protein (PrP). Complement activation is likely to contribute to neuronal damage in the end stages of prion diseases, but is also thought to participate in the initial infection, dissemination and replication stages. Infectious prion particles are likely to bind C1q and activate the complement system. Bound complement proteins may then influence the uptake and transport of prion particles by dendritic cells (DCs) and their subsequent proliferation at sites such as follicular DCs.

Original languageEnglish
Pages (from-to)355-362
Number of pages8
JournalImmunobiology
Volume212
Issue number4-5
DOIs
Publication statusPublished - Jun 26 2007
Externally publishedYes

Keywords

  • Alzheimer
  • Amyloid
  • C1q
  • Prion
  • Scrapie
  • Transmissible spongiform encephalopathy

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Hematology

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