Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
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DOI：
10.1126/science.1066371
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发表时间：
2001-12-07
期刊：
影响因子：
56.9
通讯作者：
Weis, WI
中科院分区：
文献类型：
--
作者：
Feinberg, H;Mitchell, DA;Weis, WI
树突状细胞特异性细胞内粘附分子-3 （ICAM-3）捕获非整合素（DC-SIGN）是一种存在于树突状细胞表面的c型凝集素，通过与ICAM-3结合介导树突状细胞与T细胞的初始相互作用。DC-SIGN和DC-SIGNR是在肝窦内皮、胎盘毛细血管和淋巴结上发现的相关受体，它们与存在于人类免疫缺陷病毒（HIV）包膜上的低聚糖结合，这种相互作用强烈地促进了病毒对T细胞的感染。DC-SIGN和DC-SIGNR与低聚糖结合的碳水化合物识别结构域的晶体结构，结合结合研究表明，这些受体选择性识别内源性高甘露糖低聚糖，可能为开发HIV预防药物提供了新的途径。
Dendritic cell specific intracellular adhesion molecule-3 (ICAM-3) grabbing nonintegrin (DC-SIGN), a C-type lectin present on the surface of dendritic cells, mediates the initial interaction of dendritic cells with T cells by binding to ICAM-3. DC-SIGN and DC-SIGNR, a related receptor found on the endothelium of Liver sinusoids, placental capillaries, and Lymph nodes, bind to oligosaccharides that are present on the envelope of human immunodeficiency virus (HIV), an interaction that strongly promotes viral infection of T cells. Crystal structures of carbohydrate-recognition domains of DC-SIGN and of DC-SIGNR bound to oligosaccharide, in combination with binding studies, reveal that these receptors selectively recognize endogenous high-mannose oligosaccharides and may represent a new avenue for developing HIV prophylactics.