Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion

Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors 1 – 4 , followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are...

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Bibliographic Details
Published in:	Nature (London) Vol. 588; no. 7837; pp. 327 - 330
Main Authors:	Benton, Donald J., Wrobel, Antoni G., Xu, Pengqi, Roustan, Chloë, Martin, Stephen R., Rosenthal, Peter B., Skehel, John J., Gamblin, Steven J.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 10.12.2020 Nature Publishing Group
Subjects:	101/28 631/326/596/4130 631/535/1258/1259 82/80 ACE2 Angiotensin-converting enzyme 2 Angiotensin-Converting Enzyme 2 - chemistry Angiotensin-Converting Enzyme 2 - metabolism Angiotensin-Converting Enzyme 2 - ultrastructure Binding Binding sites Binding sites (Biochemistry) Cell membranes Cell receptors Cell surface Cleavage Coronaviruses COVID-19 Cryoelectron Microscopy Destabilization Dissociation Electron microscopy Furin Furin - metabolism Fusion protein Genomes Glycoproteins Health aspects Humanities and Social Sciences Humans Membrane fusion Membrane Fusion - physiology Membrane proteins Membranes Microscopy Models, Molecular Monomers multidisciplinary Observations Peptides Physiological aspects Post-translation Priming Protein Binding Protein Folding Protein Subunits - chemistry Protein Subunits - metabolism Proteins Proteolysis Receptors Receptors, Coronavirus - chemistry Receptors, Coronavirus - metabolism Receptors, Coronavirus - ultrastructure Science Science (multidisciplinary) Severe acute respiratory syndrome coronavirus 2 Species classification Spike Glycoprotein, Coronavirus - chemistry Spike Glycoprotein, Coronavirus - metabolism Spike Glycoprotein, Coronavirus - ultrastructure Spike protein Trimers Viral diseases Viral proteins Viruses United Kingdom
ISSN:	0028-0836, 1476-4687, 1476-4687
Online Access:	Get full text
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