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Comprehensive characterization of N- and O- glycosylation of SARS-CoV-2 human receptor angiotensin converting enzyme 2.
Shajahan, Asif; Archer-Hartmann, Stephanie; Supekar, Nitin T; Gleinich, Anne S; Heiss, Christian; Azadi, Parastoo.
  • Shajahan A; Complex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Rd, Athens, GA 30602, USA.
  • Archer-Hartmann S; 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.
  • Heiss C; 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 ; 31(4): 410-424, 2021 05 03.
Article in English | MEDLINE | ID: covidwho-900424
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Semantic information from SemMedBD (by NLM)
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Subject
2019 novel coronavirus
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PROCESS_OF
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Homo sapiens
2. 2019 novel coronavirus CAUSES COVID-19
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2019 novel coronavirus
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CAUSES
Object
COVID-19
3. angiotensin converting enzyme 2 PART_OF Homo sapiens
Subject
angiotensin converting enzyme 2
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PART_OF
Object
Homo sapiens
4. Vitronecti PART_OF C5203676
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Vitronecti
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PART_OF
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C5203676
5. Vitronecti INTERACTS_WITH C0960880
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Vitronecti
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INTERACTS_WITH
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C0960880
6. angiotensin converting enzyme 2 INTERACTS_WITH HEK293 Cells
Subject
angiotensin converting enzyme 2
Predicate
INTERACTS_WITH
Object
HEK293 Cells
7. angiotensin converting enzyme 2 AFFECTS Virus Attachment
Subject
angiotensin converting enzyme 2
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AFFECTS
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Virus Attachment
8. angiotensin converting enzyme 2 INTERACTS_WITH Receptor
Subject
angiotensin converting enzyme 2
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INTERACTS_WITH
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Receptor
9. COVID-19 PROCESS_OF Patients
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COVID-19
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PROCESS_OF
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Patients
10. ACE2 gene|ACE2 AUGMENTS Complication
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ACE2 gene|ACE2
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AUGMENTS
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2019 novel coronavirus
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PROCESS_OF
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Homo sapiens
12. 2019 novel coronavirus CAUSES COVID-19
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2019 novel coronavirus
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CAUSES
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COVID-19
13. angiotensin converting enzyme 2 PART_OF Homo sapiens
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angiotensin converting enzyme 2
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PART_OF
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Homo sapiens
14. Vitronectin, human PART_OF 2019 novel coronavirus
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PART_OF
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15. Vitronectin, human INTERACTS_WITH angiotensin converting enzyme 2
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INTERACTS_WITH
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angiotensin converting enzyme 2
16. angiotensin converting enzyme 2 INTERACTS_WITH HEK293 Cells
Subject
angiotensin converting enzyme 2
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INTERACTS_WITH
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HEK293 Cells
17. angiotensin converting enzyme 2 AFFECTS Virus Attachment
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angiotensin converting enzyme 2
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angiotensin converting enzyme 2
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Receptors, Virus
19. COVID-19 PROCESS_OF Patients
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COVID-19
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PROCESS_OF
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Patients
20. ACE2 gene|ACE2 AUGMENTS Complication
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ACE2 gene|ACE2
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AUGMENTS
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ABSTRACT
The emergence of the coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has created the need for development of new therapeutic strategies. Understanding the mode of viral attachment, entry and replication has become a key aspect of such interventions. The coronavirus surface features a trimeric spike (S) protein that is essential for viral attachment, entry and membrane fusion. The S protein of SARS-CoV-2 binds to human angiotensin converting enzyme 2 (hACE2) for entry. Herein, we describe glycomic and glycoproteomic analysis of hACE2 expressed in HEK293 cells. We observed high glycan occupancy (73.2 to 100%) at all seven possible N-glycosylation sites and surprisingly detected one novel O-glycosylation site. To deduce the detailed structure of glycan epitopes on hACE2 that may be involved in viral binding, we have characterized the terminal sialic acid linkages, the presence of bisecting GlcNAc and the pattern of N-glycan fucosylation. We have conducted extensive manual interpretation of each glycopeptide and glycan spectrum, in addition to using bioinformatics tools to validate the hACE2 glycosylation. Our elucidation of the site-specific glycosylation and its terminal orientations on the hACE2 receptor, along with the modeling of hACE2 glycosylation sites can aid in understanding the intriguing virus-receptor interactions and assist in the development of novel therapeutics to prevent viral entry. The relevance of studying the role of ACE2 is further increased due to some recent reports about the varying ACE2 dependent complications with regard to age, sex, race and pre-existing conditions of COVID-19 patients.
Subject(s)
Keywords

Full text: Available Collection: International databases Database: MEDLINE Main subject: Polysaccharides / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / COVID-19 Type of study: Clinical Practice Guide Limits: Humans Language: English Journal: Glycobiology Journal subject: Biochemistry Year: 2021 Document Type: Article Affiliation country: Glycob

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Polysaccharides / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / COVID-19 Type of study: Clinical Practice Guide Limits: Humans Language: English Journal: Glycobiology Journal subject: Biochemistry Year: 2021 Document Type: Article Affiliation country: Glycob