Ficolins: complement-activating lectins involved in innate immunity

J Innate Immun. 2010;2(1):24-32. doi: 10.1159/000228160. Epub 2009 Jul 24.

Abstract

Ficolins are a group of oligomeric lectins with subunits consisting of both collagen-like and fibrinogen-like domains. The majority of ficolins identified in vertebrates and invertebrates to date recognize N-acetylglucosamine (GlcNAc). X-ray crystallographic analysis of human ficolins has shown that the fibrinogen-like domain binds to the N-acetylated moiety. Ficolins in serum are associated with MBL-associated serine protease (MASP). The ficolin-MASP complex binds directly to carbohydrates present on the surface of a variety of Gram-positive and Gram-negative bacteria through ficolin. Binding of the complex initiates complement activation via the lectin pathway, leading to generation of opsonic fragments of complement components, such as C3b, and to lysis of the bacteria by the membrane attack complex. Thus, serum ficolins play an important role in innate immunity.

Publication types

  • Review

MeSH terms

  • Acetylglucosamine / immunology
  • Animals
  • Complement C3b / immunology
  • Complement Membrane Attack Complex / immunology
  • Complement Pathway, Mannose-Binding Lectin / immunology*
  • Gram-Negative Bacteria / immunology
  • Gram-Positive Bacteria / immunology
  • Humans
  • Immunity, Innate / immunology*
  • Lectins / blood
  • Lectins / chemistry
  • Lectins / immunology*
  • Mannose-Binding Protein-Associated Serine Proteases / immunology
  • Mice

Substances

  • Complement Membrane Attack Complex
  • Lectins
  • ficolin
  • Complement C3b
  • Mannose-Binding Protein-Associated Serine Proteases
  • Acetylglucosamine