Rotaviruses preferentially bind O-linked sialylglycoconjugates and sialomucins.
Rotaviruses preferentially bind O-linked sialylglycoconjugates and sialomucins.
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轮状病毒优先结合 O-连接唾液酸糖缀合物和唾液酸粘蛋白。
DOI：
10.1093/glycob/3.5.437
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发表时间：
1993
期刊：
影响因子：
4.3
通讯作者：
Willoughby,RE
中科院分区：
文献类型：
--
作者：
Willoughby,RE
轮状病毒是全世界婴儿和儿童严重胃肠炎的最常见原因。病毒结合和进入的早期事件是细胞允许轮状病毒复制的关键决定因素。唯一已知的轮状病毒配体是唾液酸。我们现在报道猿轮状病毒优先结合唾液酸化糖缀合物的子集，即含有O-连接唾液酸部分的糖蛋白。轮状病毒能够区分以新糖脂形式存在的唾液酸化三糖配体。轮状病毒的较高亲和力结合是通过与聚集的唾液酸部分的多价结合来解释的。我们的体外数据被扩展以解释粘蛋白在轮状病毒疾病小鼠模型中的保护作用以及轮状病毒与幼鼠肠道中高分子量唾液酸粘蛋白的特异性结合。轮状病毒与唾液粘蛋白的结合可能类似于选择素介导的细胞粘附机制，并且可能有利于肠道动态环境中的病毒。
Rotaviruses are the most common cause of severe gastroenteritis in infants and children worldwide. Early events of virus binding and entry are the critical determinants of cellular permissiveness to rotavirus replication. The only known ligands for rotaviruses are sialic acids. We now report that simian rotaviruses bind preferentially to a subset of sialylated glycoconjugates, i.e. glycoproteins containing O-linked sialic acid moieties. Rotaviruses are able to distinguish between sialylated trisaccharide ligands presented as neoglycolipids. Higher avidity binding by rotaviruses is explained by multivalent binding to clustered sialic acid moieties. Ourin vitrodata are extended to explain the protective effect of mucins in the murine model of rotavirus disease and the specific binding by rotavirus to a high molecular weight sialomucin in the infant mouse intestine. Rotavirus binding to a sialomucin may be analogous to selectin-mediated mechanisms of cellular adhesion, and may be advantageous to the virus in the dynamic environment of the intestine.