Abstract
The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, via its receptor-binding domains interaction with the glycoprotein angiotensin-converting enzyme 2 on human cell surfaces. We therefore utilized an integrated glycomic and glycoproteomic analytical strategy to characterize both N- and O- glycan site-specific glycosylation within the receptor-binding domain. We demonstrate the presence of complex-type N-glycans with unusual fucosylated LacdiNAc at both sites N331 and N343 and a single site of O-glycosylation on T323.
Keywords:
SARS-CoV-2; glycoproteomics; mass spectrometry; spike glycoprotein.
© The Author(s) 2020. Published by Oxford University Press.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Angiotensin-Converting Enzyme 2 / chemistry
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Angiotensin-Converting Enzyme 2 / metabolism
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Binding Sites / genetics
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COVID-19 / metabolism
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COVID-19 / virology*
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Carbohydrate Conformation
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Carbohydrate Sequence
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Glycomics
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Glycosylation
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HEK293 Cells
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Host Microbial Interactions
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Humans
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Pandemics
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Protein Binding
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Protein Interaction Domains and Motifs
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Proteomics
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Receptors, Virus / chemistry
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Receptors, Virus / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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SARS-CoV-2* / chemistry
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SARS-CoV-2* / genetics
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SARS-CoV-2* / metabolism
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Spike Glycoprotein, Coronavirus / chemistry*
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Spike Glycoprotein, Coronavirus / genetics
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Spike Glycoprotein, Coronavirus / metabolism*
Substances
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Receptors, Virus
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Recombinant Proteins
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Spike Glycoprotein, Coronavirus
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spike protein, SARS-CoV-2
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ACE2 protein, human
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Angiotensin-Converting Enzyme 2