Dpto Biología Estructural y Química, Centro de Investigaciones Biológicas, CIB-CSIC, C/Ramiro de Maeztu 9, 28040, Madrid, Spain.
Key Laboratory of Systems Biomedicine (Ministry of Education), Shanghai Center for Systems Biomedicine, Shanghai Jiao Tong University, 800 Dongchuan Road, Shanghai, 200240, China.
Angew Chem Int Ed Engl. 2018 Nov 12;57(46):15051-15055. doi: 10.1002/anie.201807162. Epub 2018 Oct 17.
Long-chain multiantenna N-glycans are extremely complex molecules. Their inherent flexibility and the presence of repetitions of monosaccharide units in similar chemical environments hamper their full characterization by X-ray diffraction or standard NMR methods. Herein, the successful conformational and interaction analysis of a sialylated tetradecasaccharide N-glycan presenting two LacNAc repetitions at each arm is presented. This glycan has been identified as the receptor of the hemagglutinin protein of pathogenic influenza viruses. To accomplish this study, a N-glycan conjugated with a lanthanide binding tag has been synthesized, enabling analysis of the system by paramagnetic NMR. Under paramagnetic conditions, the NMR signals of each sugar unit in the glycan have been determined. Furthermore, a detailed binding epitope of the tetradecasaccharide N-glycan in the presence of HK/68 hemagglutinin is described.
长链多天线 N-聚糖是极其复杂的分子。它们固有的灵活性和在相似化学环境中重复出现的单糖单元，阻碍了它们通过 X 射线衍射或标准 NMR 方法的完全表征。本文介绍了一种成功的唾液酸十四糖 N-聚糖的构象和相互作用分析，该聚糖在每个臂上都有两个 LacNAc 重复。这种聚糖已被确定为致病性流感病毒血凝素蛋白的受体。为了完成这项研究，合成了一种与镧系元素结合标签偶联的 N-聚糖，通过顺磁 NMR 分析该系统。在顺磁条件下，确定了聚糖中每个糖单元的 NMR 信号。此外，还描述了十四糖 N-聚糖在 HK/68 血凝素存在下的详细结合表位。
