Cell surface ligands for rotavirus: mouse intestinal glycolipids and synthetic carbohydrate analogs.
Cell surface ligands for rotavirus: mouse intestinal glycolipids and synthetic carbohydrate analogs.
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轮状病毒的细胞表面配体：小鼠肠道糖脂和合成碳水化合物类似物。
DOI：
10.1016/0042-6822(92)90917-e
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发表时间：
1992
期刊：
影响因子：
3.7
通讯作者：
Yolken,RH
中科院分区：
文献类型：
--
作者：
Srnka,CA;Tiemeyer,M;Gilbert,JH;Moreland,M;Schweingruber,H;deLappe,BW;James,PG;Gant,T;Willoughby,RE;Yolken,RH
轮状病毒与小肠上皮细胞受体的结合被认为是感染过程中的关键事件，可能是碳水化合物介导的。用薄层层析法和微量滴定孔吸附法测定了轮状病毒SA 11株与小鼠小肠糖脂和真实糖脂的体外结合。与轮状病毒结合的中性小鼠肠糖脂为GA 1（Galβ1 → 3GaINAcβ1 → 4Galβ1 4Glc β1 → 1-神经酰胺）和末端为N-乙酰半乳糖胺的五糖基神经酰胺，而与轮状病毒结合的酸性脂质包括胆固醇3-硫酸酯和两种称为条带80和81的化合物。用神经酰胺聚糖酶消化表明条带80和81具有乳糖基神经酰胺核心和未鉴定的酸性部分。测试的含唾液酸的糖脂在病毒结合中没有活性。条带81可能具有神经节核心，以最大的亲合力结合轮状病毒，其次是GA 1。在测定的真实糖脂中，仅GA 1和GA 2（GaINAcβ1 → 4Galβ1 → 4Glc β1 → 1-神经酰胺）显示轮状病毒结合。GA 2结合轮状病毒的含磷脂酰乙醇酰胺二棕榈酰的新糖脂类似物，亲合力与天然GA 2相似。用β1 → 4-连接的GlcNAc或β1 → 3-连接的GaINAc取代GA 2新糖脂的末端GaINAc支持轮状病毒的结合，而其它取代则使其丧失。
Rotaviral binding to receptors on epithelial cells in the small intestine is thought to be a key event in the infection process and may be carbohydrate-mediated. Strain SA11 of rotavirus boundin vitroboth to glycolipids isolated from mouse small intestine and to authentic glycolipids using thin layer chromatography overlay and microtiter well adsorption assays. Neutral mouse intestinal glycolipids which bound rotavirus were GA1 (Galβ1 → 3GaINAcβ1 → 4Galβ1 4GIcβ1 → 1-ceramide) and pentaosylceramides with terminal N-acetylgalactosamine, while acidic lipids which bound rotavirus included cholesterol 3-sulfate and two compounds termed bands 80 and 81. Digestion with ceramide glycanase suggested that bands 80 and 81 have lactosyl ceramide cores and an unidentified acidic moiety(s). No sialic-acid-containing glycolipids tested were active in viral binding. Band 81, which may have a ganglio core, bound rotavirus with greatest avidity, followed by GA1. Of authentic glycolipids assayed, only GA1 and GA2 (GaINAcβ1 → 4Galβ1 → 4GIcβ1 → 1-ceramide) displayed rotaviral binding. A phosphatidylethanolamide dipalmitoyl-containing neoglycolipid analog of GA2 bound rotavirus with avidity similar to native GA2. Substitution of β1 → 4-linked GIcNAc or β1 → 3-linked GaINAc for terminal GaINAc of GA2 neoglycolipid supported rotaviral binding, while other substitutions abrogated it. These findings suggest that a carbohydrate epitope similar to that of GA2 is sufficient forin vitrorotaviral binding, although binding may be enhanced by galactose and/or an acidic moiety in a secondary epitope.