Lessons learned from mice deficient in lectin complement pathway molecules

Mol Immunol. 2014 Oct;61(2):59-68. doi: 10.1016/j.molimm.2014.07.007. Epub 2014 Jul 22.

Abstract

The lectin pathway of the complement system is initiated when the pattern-recognition molecules, mannose-binding lectin (MBL), ficolins or collectin-11, bind to invading pathogens or damaged host cells. This leads to activation of MBL/ficolin/collectin-11 associated serine proteases (MASPs), which in turn activate downstream complement components, ultimately leading to elimination of the pathogen. Mice deficient in the key molecules of lectin pathway of complement have been generated in order to build knowledge of the molecular mechanisms of the lectin pathway in health and disease. Despite differences in the genetic arrangements of murine and human orthologues of lectin pathway molecules, the knockout mice have proven to be valuable models to explore the effect of deficiency states in humans. In addition, new insight and unexpected findings on the diverse roles of lectin pathway molecules in complement activation, pathogen infection, coagulation, host tissue injury and developmental biology have been revealed by in vivo investigations. This review provides an overview of the mice deficient in lectin pathway molecules and highlights some of the most important findings that have resulted from studies of these.

Keywords: Complement; Ficolin; Knockout mice; Lectin pathway; MASP; Mannose-binding lectin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Complement Pathway, Mannose-Binding Lectin / physiology*
  • Humans
  • Lectins / genetics
  • Lectins / metabolism
  • Mannose-Binding Lectins / genetics
  • Mannose-Binding Lectins / metabolism
  • Mannose-Binding Protein-Associated Serine Proteases / genetics
  • Mannose-Binding Protein-Associated Serine Proteases / metabolism
  • Mice
  • Mice, Knockout

Substances

  • Lectins
  • Mannose-Binding Lectins
  • ficolin
  • Mannose-Binding Protein-Associated Serine Proteases