Institute of Chemistry and Metabolomics, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany.
Institute of Virology and Cell Biology, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany.
Viruses. 2021 Mar 5;13(3):416. doi: 10.3390/v13030416.
Glycan-protein interactions are highly specific yet transient, rendering glycans ideal recognition signals in a variety of biological processes. In human norovirus (HuNoV) infection, histo-blood group antigens (HBGAs) play an essential but poorly understood role. For murine norovirus infection (MNV), sialylated glycolipids or glycoproteins appear to be important. It has also been suggested that HuNoV capsid proteins bind to sialylated ganglioside head groups. Here, we study the binding of HBGAs and sialoglycans to HuNoV and MNV capsid proteins using NMR experiments. Surprisingly, the experiments show that none of the norovirus P-domains bind to sialoglycans. Notably, MNV P-domains do not bind to any of the glycans studied, and MNV-1 infection of cells deficient in surface sialoglycans shows no significant difference compared to cells expressing respective glycans. These findings redefine glycan recognition by noroviruses, challenging present models of infection.
糖蛋白相互作用具有高度特异性但又短暂，使得糖链成为各种生物过程中理想的识别信号。在人类诺如病毒（HuNoV）感染中，组织血型抗原（HBGAs）起着至关重要但尚未被充分理解的作用。对于鼠诺如病毒感染（MNV），唾液酸化糖脂或糖蛋白似乎很重要。也有人提出 HuNoV 衣壳蛋白与唾液酸化神经节苷脂的头基结合。在这里，我们使用 NMR 实验研究了 HBGAs 和唾液糖与 HuNoV 和 MNV 衣壳蛋白的结合。令人惊讶的是，实验表明，没有一种诺如病毒 P 结构域与唾液糖结合。值得注意的是，MNV P 结构域不与研究的任何聚糖结合，并且缺乏表面唾液糖的细胞中 MNV-1 的感染与表达相应聚糖的细胞相比没有明显差异。这些发现重新定义了诺如病毒的聚糖识别，对目前的感染模型提出了挑战。
