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Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2.
Shajahan, Asif; Supekar, Nitin T; Gleinich, Anne S; Azadi, Parastoo.
  • Shajahan A; Complex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Rd, Athens, GA 30602, USA.
  • Supekar NT; Complex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Rd, Athens, GA 30602, USA.
  • Gleinich AS; Complex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Rd, Athens, GA 30602, USA.
  • Azadi P; Complex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Rd, Athens, GA 30602, USA.
Glycobiology ; 30(12): 981-988, 2020 12 09.
Article in English | MEDLINE | ID: covidwho-1060393
Preprint
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Semantic information from SemMedBD (by NLM)
1. M Protei PART_OF C5203676
Subject
M Protei
Predicate
PART_OF
Object
C5203676
2. Vitronecti AUGMENTS C1721019
Subject
Vitronecti
Predicate
AUGMENTS
Object
C1721019
3. Mass Spectrometry USES High resolution
Subject
Mass Spectrometry
Predicate
USES
Object
High resolution
4. M Protein, multiple myeloma PART_OF 2019 novel coronavirus
Subject
M Protein, multiple myeloma
Predicate
PART_OF
Object
2019 novel coronavirus
5. Vitronectin, human AUGMENTS Virus Attachment
Subject
Vitronectin, human
Predicate
AUGMENTS
Object
Virus Attachment
6. Mass Spectrometry USES High resolution
Subject
Mass Spectrometry
Predicate
USES
Object
High resolution
ABSTRACT
The current emergence of the novel coronavirus pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) demands the development of new therapeutic strategies to prevent rapid progress of mortalities. The coronavirus spike (S) protein, which facilitates viral attachment, entry and membrane fusion is heavily glycosylated and plays a critical role in the elicitation of the host immune response. The spike protein is comprised of two protein subunits (S1 and S2), which together possess 22 potential N-glycosylation sites. Herein, we report the glycosylation mapping on spike protein subunits S1 and S2 expressed on human cells through high-resolution mass spectrometry. We have characterized the quantitative N-glycosylation profile on spike protein and interestingly, observed unexpected O-glycosylation modifications on the receptor-binding domain of spike protein subunit S1. Even though O-glycosylation has been predicted on the spike protein of SARS-CoV-2, this is the first report of experimental data for both the site of O-glycosylation and identity of the O-glycans attached on the subunit S1. Our data on the N- and O-glycosylation are strengthened by extensive manual interpretation of each glycopeptide spectra in addition to using bioinformatics tools to confirm the complexity of glycosylation in the spike protein. The elucidation of the glycan repertoire on the spike protein provides insights into the viral binding studies and more importantly, propels research toward the development of a suitable vaccine candidate.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Polysaccharides / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Type of study: Clinical Practice Guide Topics: Vaccines Limits: Humans Language: English Journal: Glycobiology Journal subject: Biochemistry Year: 2020 Document Type: Article Affiliation country: Glycob

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Polysaccharides / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Type of study: Clinical Practice Guide Topics: Vaccines Limits: Humans Language: English Journal: Glycobiology Journal subject: Biochemistry Year: 2020 Document Type: Article Affiliation country: Glycob