tetano
Editor, Senior Moderator
Anal Chem
. 2021 Jul 20.
doi: 10.1021/acs.analchem.0c04634. Online ahead of print.
Comprehensive O-Glycosylation Analysis of the SARS-CoV-2 Spike Protein with Biomimetic Trp-Arg Materials
Xuefang Dong[SUP] 1 [/SUP], Cheng Chen[SUP] 1 [/SUP], Jingyu Yan[SUP] 1 [/SUP], Xiaofei Zhang[SUP] 1 [/SUP], Xiuling Li[SUP] 1 [/SUP], Xinmiao Liang[SUP] 1 [/SUP]
Affiliations
Abstract
The COVID-19 pandemic caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is a serious public health threat. Most vaccines against SARS-CoV-2 target the highly glycosylated spike protein (S). A good knowledge of the glycosylation profile of this protein is key to successful vaccine development. Unlike the 22 confirmed N-glycosylation sites on SARS-CoV-2 S, only a few O-glycosylation sites on this protein have been reported. This difference is mainly ascribed to the extremely low stoichiometry of O-glycosylation. Herein, we designed the biomimetic materials, Trp-Arg (WR) monomer-grafted silica microspheres (designated as WR-SiO[SUB]2[/SUB]), and these biomimetic materials can enrich N- and O-linked glycopeptides with high selectivity. And WR-SiO[SUB]2[/SUB] can resist the nonglycopeptides' interference with the 100 molar fold of BSA during O-linked glycopeptide enrichment. We utilized WR-SiO[SUB]2[/SUB] to comprehensively analyze the O-glycosylation profile of recombinant SARS-CoV-2 S. Twenty-seven O-glycosylation sites including 18 unambiguous sites are identified on SARS-CoV-2 S. Our study demonstrates that the biomimetic polymer can offer specific selectivity for O-linked glycopeptides and pave the way for O-glycosylation research in biological fields. The O-glycosylation profile of SARS-CoV-2 S might supplement the comprehensive glycosylation in addition to N-glycosylation of SARS-CoV-2 S.
. 2021 Jul 20.
doi: 10.1021/acs.analchem.0c04634. Online ahead of print.
Comprehensive O-Glycosylation Analysis of the SARS-CoV-2 Spike Protein with Biomimetic Trp-Arg Materials
Xuefang Dong[SUP] 1 [/SUP], Cheng Chen[SUP] 1 [/SUP], Jingyu Yan[SUP] 1 [/SUP], Xiaofei Zhang[SUP] 1 [/SUP], Xiuling Li[SUP] 1 [/SUP], Xinmiao Liang[SUP] 1 [/SUP]
Affiliations
- PMID: 34284575
- DOI: 10.1021/acs.analchem.0c04634
Abstract
The COVID-19 pandemic caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is a serious public health threat. Most vaccines against SARS-CoV-2 target the highly glycosylated spike protein (S). A good knowledge of the glycosylation profile of this protein is key to successful vaccine development. Unlike the 22 confirmed N-glycosylation sites on SARS-CoV-2 S, only a few O-glycosylation sites on this protein have been reported. This difference is mainly ascribed to the extremely low stoichiometry of O-glycosylation. Herein, we designed the biomimetic materials, Trp-Arg (WR) monomer-grafted silica microspheres (designated as WR-SiO[SUB]2[/SUB]), and these biomimetic materials can enrich N- and O-linked glycopeptides with high selectivity. And WR-SiO[SUB]2[/SUB] can resist the nonglycopeptides' interference with the 100 molar fold of BSA during O-linked glycopeptide enrichment. We utilized WR-SiO[SUB]2[/SUB] to comprehensively analyze the O-glycosylation profile of recombinant SARS-CoV-2 S. Twenty-seven O-glycosylation sites including 18 unambiguous sites are identified on SARS-CoV-2 S. Our study demonstrates that the biomimetic polymer can offer specific selectivity for O-linked glycopeptides and pave the way for O-glycosylation research in biological fields. The O-glycosylation profile of SARS-CoV-2 S might supplement the comprehensive glycosylation in addition to N-glycosylation of SARS-CoV-2 S.