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Analysis of SARS-CoV-2 S and human ACE2 protein by LC-MS

ABSTRACT: Analysis of intact N-linked glycopeptides for SARS-Cov-2 S and huamn ACE2 protein by LC-MS

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Severe Acute Respiratory Syndrome Coronavirus 2

TISSUE(S): Epithelial Cell

SUBMITTER: Peng Zhao

LAB HEAD: Lance Wells

PROVIDER: PXD019937 | Pride | 2020-09-09

REPOSITORIES: Pride

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			Action	DRS
	LZ-20200402-Chen-S-Degraded-Glypep-TASVc-AV5pmol-SemiTASVcQpE.txt	Txt
	LZ-20200402-Chen-S-Degraded-Glypep-TASVc-AV5pmol.raw	Raw
	LZ-20200402-Chen-S-Degraded-Glypep-YFWLc-AV5pmol-SemiYFWLcQpE.txt	Txt
	LZ-20200402-Chen-S-Degraded-Glypep-YFWLc-AV5pmol.raw	Raw
	LZ-20200403-Chen-S-Degraded-Glypep-KREc-AV5pmol-SemiKREcQpE.txt	Txt

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Publications

Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor.

Zhao Peng P Praissman Jeremy L JL Grant Oliver C OC Cai Yongfei Y Xiao Tianshu T Rosenbalm Katelyn E KE Aoki Kazuhiro K Kellman Benjamin P BP Bridger Robert R Barouch Dan H DH Brindley Melinda A MA Lewis Nathan E NE Tiemeyer Michael M Chen Bing B Woods Robert J RJ Wells Lance L

Cell host & microbe 20200824 4

The SARS-CoV-2 betacoronavirus uses its highly glycosylated trimeric Spike protein to bind to the cell surface receptor angiotensin converting enzyme 2 (ACE2) glycoprotein and facilitate host cell entry. We utilized glycomics-informed glycoproteomics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existi ...[more]

PMID: 32841605

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Analysis of SARS-CoV-2 S and human ACE2 protein by LC-MS

Project description:Analysis of deglycosylated N-linked glycopeptides for SARS-Cov-2 S and human ACE2 protein by LC-MS

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Project description:Reanalysis of submissions PXD005411, PXD005413, PXD005412, PXD005553, PXD005555, PXD005565 and PXD019937 using Glyco-Decipher. Identification results of peptide-spectrum matches supporting Glyco-Decipher manuscript (Glyco-Decipher: glycan database-independent peptide matching enables discovery of new glycans and in-depth characterization of site-specific N-glycosylation). Recently, several elegant bioinformatics tools have been developed to identify glycopeptides from tandem mass spectra for site-specific glycoproteomics studies. These glycan database-dependent tools have substantially improved glycoproteomics analysis but fail to identify glycopeptides with unexpected glycans. We present a platform called Glyco-Decipher to interpret the glycoproteomics data of N-linked glycopeptides. It adopts a glycan database-independent peptide matching scheme that allows the unbiased profiling of glycans and the discovery of new glycans linked with modifications. Reanalysis of several large-scale datasets showed that Glyco-Decipher outperformed the open search method in glycan blind searching and the popular glycan database-dependent software tools in glycopeptide identification. Our glycan database-independent search also revealed that modified glycans are responsible for a large fraction of unassigned glycopeptide spectra in shotgun glycoproteomics.

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Analysis of SARS-CoV-2 S and human ACE2 protein by LC-MS

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RNAseq analyses in HEK293T-ACE2 cells infected with SARS-CoV-2 (VOC Delta, 24hours) vs untreated cells

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