Proteomics

Dataset Information

0

Deciphering the O-glycosylation of HKU1 Spike Protein with the Dual-Functional Hydrophilic Interaction Chromatography Materials


ABSTRACT: HKU1 is a human betacoronavirus and infects host cells via highly glycosylated spike protein (S). At present, N-glycosylation of HKU1 S has been reported, however, little is known about its O-glycosylation, which hinders an 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 materials (HBS). The enrichment method for O-glycopeptides with HBS was developed and validated using standard proteins. The application of the developed method to HKU1 S1 subunit resulted in 61 novel O-glycosylation sites, among which 56% were predicted to be exposed on protein outer surface. Moreover, the O-linked glycans and their abundance on each HKU1 S1 site were also analyzed. The obtained O-glycosylation dataset would provide valuable insights for the understanding of the structure of HKU1 S.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Human Coronavirus Hku1 (isolate N1)

TISSUE(S): T Cell, Cell Culture

DISEASE(S): Severe Acute Respiratory Syndrome

SUBMITTER: Dongmei Fu  

LAB HEAD: Dongmei Fu

PROVIDER: PXD025967 | Pride | 2022-02-17

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20201015_HKU_1_2_rare.mgf Mgf
20201015_HKU_1_2_rare.mzid.gz Mzid
20201015_HKU_1_2_rare_1_.mgf Mgf
20201015_HKU_1_2_rare_1_.mzid.gz Mzid
20201015_HKU_1_2_rare_2_.mgf Mgf
Items per page:
1 - 5 of 37
altmetric image

Publications

Deciphering the O-Glycosylation of HKU1 Spike Protein With the Dual-Functional Hydrophilic Interaction Chromatography Materials.

Cui Yun Y   Dong Xuefang X   Zhang Xiaofei X   Chen Cheng C   Fu Dongmei D   Li Xiuling X   Liang Xinmiao X  

Frontiers in chemistry 20210813


HKU1 is a human beta coronavirus and infects host cells <i>via</i> 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 usi  ...[more]

Similar Datasets

2013-07-15 | E-GEOD-48429 | biostudies-arrayexpress
2023-04-06 | PXD033779 | Pride
2023-10-24 | PXD040613 | Pride
2023-01-05 | PXD037182 | Pride
| S-EPMC6641700 | biostudies-literature
2021-11-03 | PXD022896 | Pride
| PRJNA69669 | ENA
2024-01-26 | PXD041282 | Pride
2022-02-16 | PXD029218 | Pride
2018-11-25 | E-MTAB-7384 | biostudies-arrayexpress