Deciphering the O-Glycosylation of HKU1 Spike Protein With the Dual-Functional Hydrophilic Interaction Chromatography Materials.
Deciphering the O-Glycosylation of HKU1 Spike Protein With the Dual-Functional Hydrophilic Interaction Chromatography Materials.
复制标题
使用双功能亲水相互作用色谱材料破译 HKU1 刺突蛋白的 O-糖基化。
DOI：
10.3389/fchem.2021.707235
复制
发表时间：
2021
影响因子：
5.5
通讯作者：
Liang X
中科院分区：
文献类型：
--
作者：
Cui Y;Dong X;Zhang X;Chen C;Fu D;Li X;Liang X
HKU 1是一种人β冠状病毒，通过高度糖基化的刺突蛋白（S）感染宿主细胞。已经报道了HKU 1 S的N-糖基化。然而，对其O-糖基化的研究甚少，这阻碍了对其生物学功能的深入了解。本文基于双功能组氨酸键合硅胶（HBS）材料对HKU 1 S的O-糖基化进行了全面的研究。开发了用HBS富集O-糖肽的方法，并使用标准蛋白进行了验证。将所开发的方法应用于HKU 1 S1亚基导致46个新的O-糖基化位点，其中55.6%被预测暴露在外蛋白表面上。此外，还分析了每个HKU 1 S1位点上的O-连接聚糖及其丰度。所获得的O-糖基化数据集将为HKU 1 S的结构提供有价值的见解。
HKU1 is a human beta coronavirus and infects host cells via highly glycosylated spike protein (S). The N-glycosylation of HKU1 S has been reported. However, little is known about its O-glycosylation, which hinders the in-depth understanding of its biological functions. Herein, a comprehensive study of O-glycosylation of HKU1 S was carried out based on dual-functional histidine-bonded silica (HBS) materials. The enrichment method for O-glycopeptides with HBS was developed and validated using standard proteins. The application of the developed method to the HKU1 S1 subunit resulted in 46 novel O-glycosylation sites, among which 55.6% were predicted to be exposed on the outer protein surface. Moreover, the O-linked glycans and their abundance on each HKU1 S1 site were analyzed. The obtained O-glycosylation dataset will provide valuable insights into the structure of HKU1 S.