Dataset Information

Structural- and Site-specific N-glycosylation Characterization of COVID-19 Virus Spike with StrucGP

ABSTRACT: Spike (S) protein plays a key role in COVID-19 (SARS-CoV-2) infection and host-cell entry. Previous studies have systematically analyzed site-specific glycans compositions of S protein. Here, we further provide structure-clear N-glycosylation of S protein at site-specific level by using our recently developed structure- and site-specific N-glycoproteomics sequencing algorithm StrucGP. In addition to the common N-glycans as detected in previous studies, many uncommon glycosylation structures such as LacdiNAc structures, Lewis structures, Mannose 6-Phosphate (M6P) residues and bisected core structures were unambiguously mapped at a total of 20 glycosites in the S protein trimer and protomer. These data further supports the glycosylation structural-functional investigations of COVID-19 virus Spike.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Early Embryonic Cell

DISEASE(S): Influenza

SUBMITTER: Bojing Zhu

LAB HEAD: Shisheng Sun

PROVIDER: PXD034086 | Pride | 2022-10-13

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Zhu_S_protomer_GluC_50cm_4h_1.raw	Raw
	Zhu_S_protomer_GluC_50cm_4h_1.xlsx	Xlsx
	Zhu_S_protomer_GluC_50cm_4h_2.raw	Raw
	Zhu_S_protomer_GluC_50cm_4h_2.xlsx	Xlsx
	Zhu_S_protomer_GluC_50cm_4h_3.raw	Raw

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Publications

Structural- and Site-Specific N-Glycosylation Characterization of COVID-19 Virus Spike with StrucGP.

Zhu Bojing B Chen Zexuan Z Shen Jiechen J Xu Yintai Y Lan Rongxia R Sun Shisheng S

Analytical chemistry 20220829 36

The spike (S) protein plays a key role in COVID-19 (SARS-CoV-2) infection and host-cell entry. Previous studies have systematically analyzed site-specific glycan compositions as well as many important structural motifs of the S protein. Here, we further provide structural-clear N-glycosylation of the S protein at a site-specific level by using our recently developed structural- and site-specific N-glycoproteomics sequencing algorithm, StrucGP. In addition to the common N-gly ...[more]

PMID: 36036581

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Project description:Recombinant proteins are of great interest in glycobiology and proteomics, known especially for their reproducibility and accessibility. However, variation in glycosylation among recombinant glycoproteins is not well understood and may depend on numerous conditions in the biomanufacturing process. In order to confidently assess variation in glycosylation measurements, it is vital to both optimize the measurement of, and determine the degree of variation between, distributions of glycosylation on specific sites of glycoproteins. This is especially important for glycoproteins that are known to have rapid sequence changes, such as with different influenza strains. In this study, eight strains of recombinant influenza hemagglutinin and neuraminidase produced from HEK293 cell line were obtained from four vendors and digestion was conducted using a series of complex multi-enzymatic methods designed to isolate glycopeptide sequons. Site-specific glycosylation profiles of intact glycopeptides were produced using mass spectrometric evaluation on an orbitrap system and compared using spectral similarity scores. Variation in glycan abundances and distribution was most pronounced between different strains of virus (similarity score = 383 out of 1000), whereas replicates resulted in low variation (similarity score = 957 out of 1000). Glycan variation was also measured based on differences between vendors, lots, batches, protease digestion, and intra-protein site. The most abundant glycans in all of these influenza glycoproteins were monofucosylated and complex, as reported by other laboratories. However, it was found that different vendors can produce very different glycan distributions for the same glycosylation site. Notably, it is demonstrated that glycan distributions are similar for conserved regions of influenza glycoproteins. Overall, these methods present a potential use in developing reproducible measurements of glycosylated biologics for quality control or making more informed decisions in biomanufacturing.

Dataset Information

Structural- and Site-specific N-glycosylation Characterization of COVID-19 Virus Spike with StrucGP

Dataset's files

Publications

Structural- and Site-Specific <i>N-</i>Glycosylation Characterization of COVID-19 Virus Spike with StrucGP.

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