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SARS-CoV-2 spike protein glycosylation enriched by HILIC and Ti-IMAC

ABSTRACT: In this work, we performed a fully descriptive analysis N- and O- linked glycosylation of SARS-COV-2 S glycoprotein. We investigated that dual-functionalized Ti-IMAC material enable the simultaneous enrichment and separation of neutral and sialyl glycopeptides of a recombinant SARS-CoV-2 S glycoprotein from HEK293, which will eliminate the signal suppression of neutral glycopeptides to sialyl glycopeptides and improve the glycoform coverage of S protein. We have profiled 19 of its 22 potential N-glycosylated sites with 398 unique glycoforms in dual-functional Ti-IMIAC approach that is 1.6-fold of that in conventional HILIC method. We also identified O-linked glycosylation site that was not found in dual-functional Ti-IMIAC approach. In addition, we have also identified mannose-6-phosphate (M6P) glycosylation, which substantially expands the current knowledge of the spike protein’s glycosylation and enables the investigation of the influence of mannose-6-Phosphate on its cell entry.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Junfeng Huang

LAB HEAD: Lingjun Li

PROVIDER: PXD026450 | Pride | 2022-01-11

REPOSITORIES: pride

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			Action	DRS
	20201208_SARS_COV_2_S_Ty_CTy_HILIC_HCD_1.byrslt	Other
	20201208_SARS_COV_2_S_Ty_CTy_TiIMAC_FA_HCD_1.byrslt	Other
	20201208_SARS_COV_2_S_Ty_CTy_TiIMAC_TFA_HCD_1.byrslt	Other
	20201208_S_HILIC_2_0_5ug_1.raw	Raw
	20201208_S_HILIC_2_0_5ug_1_Byonic_results.xlsx	Xlsx

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