Dataset Information

Site-specific glycosylation patterns of SARS-CoV-2 spike derived from recombinant protein and viral WA1 and D614G strains

ABSTRACT: We have characterized the site-specific glycosylation patterns of the HEK293 recombinant spike RBD and S1 domains as well as the intact spike derived from whole virus produced in Vero cells.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Cercopithecus Aethiops (green Monkey) (grivet) Homo Sapiens (human)

TISSUE(S): Early Embryonic Cell

DISEASE(S): Covid-19

SUBMITTER: Yuan Tian

LAB HEAD: John F. Cipollo

PROVIDER: PXD029218 | Pride | 2022-02-16

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	D614G_pre2_PNGaseF_20210128_Rep1.raw	Raw
	D614G_pre2_PNGaseF_20210128_Rep2.raw	Raw
	D614G_pre2_PNGaseF_20210128_Rep3.raw	Raw
	D614G_prep1_E50-60_HCD_Rep_Nglycan.blgc	Other
	D614G_prep1_E50_HCD_Rep1.raw	Raw

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Publications

Site-Specific Glycosylation Patterns of the SARS-CoV-2 Spike Protein Derived From Recombinant Protein and Viral WA1 and D614G Strains.

Tian Yuan Y Parsons Lisa M LM Jankowska Ewa E Cipollo John F JF

Frontiers in chemistry 20211119

The SARS-CoV-2 spike protein is heavily glycosylated, having 22 predicted N-glycosylation sites per monomer. It is also O-glycosylated, although the number of O-glycosites is less defined. Recent studies show that spike protein glycans play critical roles in viral entry and infection. The spike monomer has two subdomains, S1 and S2, and a receptor-binding domain (RBD) within the S1 domain. In this study, we have characterized the site-specific glycosylation patterns of the HEK293 recombinant spi ...[more]

PMID: 34869209

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