Institute of Medical Virology, University of Zurich, Zurich, Switzerland.
Institute of Medical Virology, University of Zurich, Zurich, Switzerland
J Virol. 2020 Jan 31;94(4). doi: 10.1128/JVI.01357-19.
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.
甲型流感病毒(IAV)包膜蛋白血凝素作为宿主细胞受体结合α2,6-或α2,3 连接的唾液酸。蝙蝠 IAV 亚型 H17N10 和 H18N11 是此规则的例外,它们不结合唾液酸,而是通过主要组织相容性复合体(MHC)II 类进入细胞。在这里,我们回顾了 IAV 受体的现有知识,重点介绍了影响 IAV 附着和内化的糖基化唾液酸变体、蛋白辅助受体和替代受体,这些受体超越了描述明确的唾液酸结合作用。