| First Author | Weis WI | Year | 1998 |
| Journal | Immunol Rev | Volume | 163 |
| Pages | 19-34 | PubMed ID | 9700499 |
| Mgi Jnum | J:48857 | Mgi Id | MGI:1275890 |
| Doi | 10.1111/j.1600-065x.1998.tb01185.x | Citation | Weis WI, et al. (1998) The C-type lectin superfamily in the immune system. Immunol Rev 163:19-34 |
| abstractText | 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. |
