Structures and distributions of SARS-CoV-2 spike proteins on intact virions

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude 1 . Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells 2 – 6 . S exhibi...

Celý popis

Uložené v:
Podrobná bibliografia
Vydané v:Nature (London) Ročník 588; číslo 7838; s. 498 - 502
Hlavní autori: Ke, Zunlong, Oton, Joaquin, Qu, Kun, Cortese, Mirko, Zila, Vojtech, McKeane, Lesley, Nakane, Takanori, Zivanov, Jasenko, Neufeldt, Christopher J., Cerikan, Berati, Lu, John M., Peukes, Julia, Xiong, Xiaoli, Kräusslich, Hans-Georg, Scheres, Sjors H. W., Bartenschlager, Ralf, Briggs, John A. G.
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: London Nature Publishing Group UK 17.12.2020
Nature Publishing Group
Predmet:
101/28
631/326/596/4130
631/535/1258/1259
631/535/1258/1260
Antibodies
Antibodies, Neutralizing - immunology
Binding sites
Cell Line, Tumor
Coronaviruses
COVID-19 - immunology
COVID-19 Vaccines - immunology
Cryoelectron Microscopy
Distribution
Electron microscopy
Endoplasmic reticulum
Enzymes
Flexibility
Humanities and Social Sciences
Humans
Infections
Lipid bilayers
Lipids
Microscopy
Models, Molecular
Monomers
multidisciplinary
Peptides
Physiological aspects
Pliability
Protein Conformation
Protein Multimerization
Protein S
Protein structure
Proteins
SARS-CoV-2 - chemistry
SARS-CoV-2 - isolation & purification
SARS-CoV-2 - metabolism
SARS-CoV-2 - ultrastructure
Science
Science (multidisciplinary)
Severe acute respiratory syndrome coronavirus 2
Spike Glycoprotein, Coronavirus - analysis
Spike Glycoprotein, Coronavirus - chemistry
Spike Glycoprotein, Coronavirus - isolation & purification
Spike Glycoprotein, Coronavirus - ultrastructure
Structure
Tomography
Transmission electron microscopy
Trimers
Virion - chemistry
Virion - isolation & purification
Virion - metabolism
Virion - ultrastructure
Virions
Viroplasm
Virus research
United Kingdom
ISSN:0028-0836, 1476-4687, 1476-4687
On-line prístup:Získať plný text
Tagy: Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
Popis
Shrnutí:Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude 1 . Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells 2 – 6 . S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes 2 , 7 , 8 . The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy 2 , 7 , 9 – 12 , but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination. Cryo-electron microscopy and tomography studies reveal the structures, conformations and distributions of spike protein trimers on intact severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions and provide a basis for understanding the interactions of the spike protein with neutralizing antibodies.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
ObjectType-Literature Review-3
content type line 23
ISSN:0028-0836
1476-4687
1476-4687
DOI:10.1038/s41586-020-2665-2