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ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV
- Source :
- Chemical communications (Cambridge, England). 57(48)
- Publication Year :
- 2021
-
Abstract
- We report a distinct difference in the interactions of the glycans of the host-cell receptor, ACE2, with SARS-CoV-2 and SARS-CoV S-protein receptor-binding domains (RBDs). Our analysis demonstrates that the ACE2 glycan at N322 enhances interactions with the SARS-CoV-2 RBD while the ACE2 glycan at N90 may offer protection against infections of both coronaviruses depending on its composition. The interactions of the ACE2 glycan at N322 with SARS-CoV RBD are blocked by the presence of the RBD glycan at N357 of the SARS-CoV RBD. The absence of this glycosylation site on SARS-CoV-2 RBD may enhance its binding with ACE2.
- Subjects :
- 2019-20 coronavirus outbreak
Glycan
Glycosylation
Coronavirus disease 2019 (COVID-19)
viruses
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
Protein domain
Plasma protein binding
Molecular Dynamics Simulation
Catalysis
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Protein Domains
Polysaccharides
Materials Chemistry
Humans
skin and connective tissue diseases
030304 developmental biology
0303 health sciences
biology
Chemistry
SARS-CoV-2
fungi
Metals and Alloys
General Chemistry
Surfaces, Coatings and Films
Electronic, Optical and Magnetic Materials
Cell biology
body regions
Severe acute respiratory syndrome-related coronavirus
Spike Glycoprotein, Coronavirus
Ceramics and Composites
biology.protein
Angiotensin-Converting Enzyme 2
hormones, hormone substitutes, and hormone antagonists
030217 neurology & neurosurgery
Protein Binding
Subjects
Details
- ISSN :
- 1364548X
- Volume :
- 57
- Issue :
- 48
- Database :
- OpenAIRE
- Journal :
- Chemical communications (Cambridge, England)
- Accession number :
- edsair.doi.dedup.....d8be8d7189fb8a72b2ec5ab82734d409