The C-type lectin superfamily in the immune system

被引:881
作者
Weis, WI [1 ]
Taylor, ME
Drickamer, K
机构
[1] Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA
[2] Univ Oxford, Dept Biochem, Glycobiol Inst, Oxford OX1 3QU, England
基金
英国惠康基金;
关键词
D O I
10.1111/j.1600-065X.1998.tb01185.x
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
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 Ca2+-dependent carbohydrate-recognition domains (C-type CRDs). Pathogen recognition by soluble collectins 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.
引用
收藏
页码:19 / 34
页数:16
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