From the Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), UMR8576 of CNRS and UdeLille, 50 Avenue de Halley, 59658 Villeneuve d'Ascq, France.
From the Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), UMR8576 of CNRS and UdeLille, 50 Avenue de Halley, 59658 Villeneuve d'Ascq, France
J Biol Chem. 2018 Jul 27;293(30):11966-11967. doi: 10.1074/jbc.H118.004336.
Human norovirus binding to histo-blood group antigens (HBGAs) is thought to direct their entry into host cells. However, the glycan epitopes characteristic of HBGAs are also present on oligosaccharides abundant in human milk. In this issue of JBC, Hanisch compared norovirus binding to human gastric mucins and human milk oligosaccharides, finding those bound most avidly are rich in α-fucose. Mimicry of these epitopes with α-fucose multivalently displayed on other carbohydrate scaffolds successfully scavenged this prevalent virus, providing new insights into norovirus biology and clues for future therapeutic development.
人们认为，诺如病毒与血型抗原（HBGAs）的结合指导其进入宿主细胞。然而，HBGAs 上具有特征性的聚糖表位也存在于人类乳中丰富的低聚糖上。在本期 JBC 中，Hanisch 比较了诺如病毒与人胃粘蛋白和人乳寡糖的结合，发现与其结合最紧密的是富含α-岩藻糖的物质。通过在其他碳水化合物支架上多价展示α-岩藻糖模拟这些表位，可以成功清除这种流行病毒，为诺如病毒生物学提供了新的见解，并为未来的治疗开发提供了线索。
