Mammalian prion or PrP^Sc is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycoprotein called the prion protein or PrP^C. Sialylation of the prion protein, a terminal modification of N-linked glycans, was discovered more than 30 years ago, yet the role of sialylation in prion pathogenesis is not well understood. This chapter summarizes current knowledge on the role of sialylation of the prion protein in prion diseases. First, we discuss recent data suggesting that sialylation of PrP^Sc N-linked glycans determines the fate of prion infection in an organism and control prion lymphotropism. Second, emerging evidence pointing out at the role N-glycans in neuroinflammation are discussed. Thirds, this chapter reviews a mechanism postulating that sialylated N-linked glycans are important players in defining strain-specific structures. A new hypothesis according to which individual strain-specific PrP^Sc structures govern selection of PrP^C sialoglycoforms is discussed. Finally, this chapter explain how N-glycan sialylation control the prion replication and strain interference. In summary, comprehensive review of our knowledge on N-linked glycans and their sialylation provided in this chapter helps to answer important questions of prion biology that have been puzzling for years.

哺乳动物病毒或PrP ^Sc是一种蛋白质感染剂，由被称为the病毒蛋白或PrP ^C的唾液酸糖蛋白的错误折叠，自我复制状态组成。N蛋白的唾液酸化是N-连接聚糖的末端修饰，已于30多年前被发现，但是唾液酸化在病毒发病机理中的作用尚不清楚。本章总结了有关knowledge病毒蛋白的唾液酸化作用在current病毒疾病中的最新知识。首先，我们讨论最近的数据，表明PrP ^Sc的唾液酸化N-连接的聚糖决定了生物体中病毒感染的命运并控制了ion病毒的亲淋巴细胞性。第二，讨论了新的证据指出N-聚糖在神经炎症中的作用。第三，本章回顾了一种机制，认为唾液酸化的N-连接聚糖在定义菌株特异性结构中起重要作用。一个新的假说，根据该假说，个别菌株特异性的PrP ^Sc结构决定着PrP ^C的选择讨论了唾液糖型。最后，本章介绍了N-聚糖唾液酸化如何控制the病毒的复制和菌株干扰。总而言之，本章提供的有关N-连接聚糖及其唾液酸化的知识的全面综述，有助于回答困扰了多年的病毒生物学的重要问题。