Ficolins/Mannose-binding protein

From CFGparadigms

Revision as of 16:59, 6 April 2010 by Heather Buschman (Talk | contribs)
(diff) ← Older revision | Current revision (diff) | Newer revision → (diff)
Jump to: navigation, search

The ficolins share a common organization and function with the collectins: serum mannose-binding and the pulmonary surfactant proteins C and D. All of these proteins are soluble mediators of innate immunity and consist of globular sugar-binding domains attached to collagenous stalks, which can invoke innate immune responses either through complement fixation or interaction with receptors on the surfaces of macrophages. Amongst these proteins, the ficolins have been most extensively investigated with CFG resources, while mannose-binding protein is the best characterized. The ficolins have fibrinogen-like sugar-binding domains, rather than C-type carbohydrate-recognition domains, but conceptually fall within the same group.


CFG Participating Investigators contributing to the understanding of this paradigm

Participating Investigators have generated and characterized knockout mice, defined the sugar-binding properties and undertaken structural analysis for members of this glycan-binding protein (GBP) group.

  • PIs working on ficolins include: Raymond Dwek, Daniel Mitchell, Nicole Thielens
  • PIs investigating other paradigms in this GBP group include: Kurt Drickamer, Ten Feizi, Toshisuke Kawasaki, Laura Kiessling, Reiko Lee, Yuan Lee, Jamie Marth, Kenneth Ng, Michel Nussenzweig, Pauline Rudd, Maureen Taylor, Bill Weis
  • Non-PIs with who have used CFG resources to study ficolins include: David Stephens

Progress toward understanding this GBP paradigm

Carbohydrate ligands

Cellular expression


Biological roles of GBP-ligand interaction

CFG resources used in investigations

The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the CFG database search results for ficolin and mannose-binding receptor.

Glycan profiling

Glycogene microarray

Knockout mouse lines

Glycan array

The binding specificities of several of the ficolins have been analyzed and other members of the group were screened on the CFG glycan array.

Related GBPs

Serum mannose-binding protein (MBP, also designated mannose-binding lectin, MBL) and the pulmonary surfactant proteins SP-C and SP-D


  • Gout E, Garlatti V, Smith DF, Lacroix M M, Dumestre-Perard C, Lunardi T, Martin L, Cesbron JY, Arlaud GJ, Gaboriaud C, Thielens NM (2010) Carbohydrate recognition properties of human ficolins: Glycan array screening reveals the sialic acid binding specificity of M-ficolin. J Biol Chem 285, 6612-6622.
  • Krarup A, Mitchell DA, Sim RB (2008) Recognition of acetylated oligosaccharides by human L-ficolin. Immunol Lett 118, 152-6.


The CFG is grateful to the following PIs for their contributions to this wiki page: Kurt Drickamer, Yvette van Kooyk

Personal tools