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Breaking the Convention: Sialoglycan Variants, Coreceptors, and Alternative Receptors for Influenza A Virus Entry.
Journal of Virology ( IF 4.0 ) Pub Date : 2020-01-31 , DOI: 10.1128/jvi.01357-19
Umut Karakus 1 , Marie O Pohl 1 , Silke Stertz 2
Affiliation  

The influenza A virus (IAV) envelope protein hemagglutinin binds α2,6- or α2,3-linked sialic acid as a host cell receptor. Bat IAV subtypes H17N10 and H18N11 form an exception to this rule and do not bind sialic acid but enter cells via major histocompatibility complex (MHC) class II. Here, we review current knowledge on IAV receptors with a focus on sialoglycan variants, protein coreceptors, and alternative receptors that impact IAV attachment and internalization beyond the well-described sialic acid binding.

中文翻译:

打破惯例:甲流病毒变种的变体,共受体和替代受体。

甲型流感病毒(IAV)包膜蛋白血凝素结合α2,6-或α2,3-连接的唾液酸作为宿主细胞受体。Bat IAV H17N10和H18N11亚型是该规则的一个例外,不结合唾液酸,而是通过II类主要组织相容性复合体(MHC)进入细胞。在这里,我们回顾了有关IAV受体的当前知识,重点是唾液酸聚糖变体,蛋白质共受体和影响IAV附着和内化的唾液酸结合以外的替代受体。
更新日期:2019-11-01
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