The C-type lectin superfamily in the immune system

Immunol Rev. 1998 Jun;163:19-34. doi: 10.1111/j.1600-065x.1998.tb01185.x.

Abstract

Protein-carbohydrate interactions serve multiple functions in the immune system. Many animal lectins (sugar-binding proteins) mediate both pathogen recognition and cell-cell interactions using structurally related Ca(2+)-dependent carbohydrate-recognition domains (C-type CRDs). Pathogen recognition by soluble collections such as serum mannose-binding protein and pulmonary surfactant proteins, and also the macrophage cell-surface mannose receptor, is effected by binding of terminal monosaccharide residues characteristic of bacterial and fungal cell surfaces. The broad selectivity of the monosaccharide-binding site and the geometrical arrangement of multiple CRDs in the intact lectins explains the ability of the proteins to mediate discrimination between self and non-self. In contrast, the much narrower binding specificity of selectin cell adhesion molecules results from an extended binding site within a single CRD. Other proteins, particularly receptors on the surface of natural killer cells, contain C-type lectin-like domains (CTLDs) that are evolutionarily divergent from the C-type lectins and which would be predicted to function through different mechanisms.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium*
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism
  • Collectins
  • Humans
  • Immune System / metabolism
  • Killer Cells, Natural / metabolism
  • Lectins / chemistry*
  • Lectins / metabolism
  • Lectins, C-Type*
  • Mannose-Binding Lectins*
  • Molecular Sequence Data
  • Protein Conformation*
  • Receptors, Cell Surface / chemistry
  • Receptors, Cell Surface / metabolism
  • Receptors, Immunologic / chemistry
  • Selectins / metabolism

Substances

  • Carrier Proteins
  • Collectins
  • Lectins
  • Lectins, C-Type
  • Mannose-Binding Lectins
  • Receptors, Cell Surface
  • Receptors, Immunologic
  • Selectins
  • mannose receptor
  • Calcium