About: Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding

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About: Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding
Creator	Wang, Xinquan Zhou, Haixia Chen, Silian Gui, Miao Song, Wenfei Xiang, Ye Xu, Jingwei
Source	Medline; PMC
abstract	The global outbreak of SARS in 2002-2003 was caused by the infection of a new human coronavirus SARS-CoV. The infection of SARS-CoV is mediated mainly through the viral surface glycoproteins, which consist of S1 and S2 subunits and form trimer spikes on the envelope of the virions. Here we report the ectodomain structures of the SARS-CoV surface spike trimer in different conformational states determined by single-particle cryo-electron microscopy. The conformation 1 determined at 4.3 Å resolution is three-fold symmetric and has all the three receptor-binding C-terminal domain 1 (CTD1s) of the S1 subunits in “down” positions. The binding of the “down” CTD1s to the SARS-CoV receptor ACE2 is not possible due to steric clashes, suggesting that the conformation 1 represents a receptor-binding inactive state. Conformations 2-4 determined at 7.3, 5.7 and 6.8 Å resolutions are all asymmetric, in which one RBD rotates away from the “down” position by different angles to an “up” position. The “up” CTD1 exposes the receptor-binding site for ACE2 engagement, suggesting that the conformations 2-4 represent a receptor-binding active state. This conformational change is also required for the binding of SARS-CoV neutralizing antibodies targeting the CTD1. This phenomenon could be extended to other betacoronaviruses utilizing CTD1 of the S1 subunit for receptor binding, which provides new insights into the intermediate states of coronavirus pre-fusion spike trimer during infection.
has issue date	2016-12-23(xsd:dateTime)
bibo:doi	10.1038/cr.2016.152
bibo:pmid	28008928
has license	bronze-oa
sha1sum (hex)	9ebc09cec2a54ebc2629bf09e02a6c19493fc750
schema:url	https://doi.org/10.1038/cr.2016.152
resource representing a document's title	Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding
has PubMed Central identifier	PMC5223232
has PubMed identifier	28008928
schema:publication	Cell Research
resource representing a document's body	covid:9ebc09cec2a54ebc2629bf09e02a6c19493fc750#body_text
is schema:about of	named entity 'SARS-CoV' named entity 'receptor' named entity 'position' named entity 'SARS-CoV' named entity 'CONSIST' named entity 'REQUIRED' named entity 'SPIKES' named entity 'SYMMETRIC' named entity '4.3' covid:arg/9ebc09cec2a54ebc2629bf09e02a6c19493fc750 named entity 'PREREQUISITE' named entity 'ENVELOPE' named entity 'RESOLUTION' named entity 'ACE2' named entity 'BETACORONAVIRUSES' named entity 'NEW' named entity 'FORM' named entity 'SARS-COV' named entity 'VIRAL' named entity 'PARTICLE' named entity 'RBD' named entity 'ACTIVE STATE' named entity 'REPORT' named entity 'RECEPTOR' named entity 'PHENOMENON' named entity 'CORONAVIRUS' named entity 'ECTODOMAIN' named entity 'ASYMMETRIC' named entity 'AWAY' named entity 'EXTENDED' named entity 'SARS-COV' named entity 'INACTIVE STATE' named entity 'RECEPTOR BINDING' named entity 'INSIGHTS' named entity 'POSSIBLE' named entity 'STRUCTURES' named entity 'STATE' named entity 'REVEAL' named entity 'CONFORMATION' named entity 'SPIKE' named entity 'INFECTION' named entity 'SINGLE' named entity 'HERE' named entity 'POSITIONS' named entity 'NEUTRALIZING ANTIBODIES' named entity 'CONFORMATIONAL CHANGE' named entity 'DUE TO' named entity 'FOLD' named entity 'C-TERMINAL' named entity 'DIFFERENT' named entity 'TRIMER' named entity 'VIRIONS' named entity 'PRE' named entity 'ANGLES' named entity 'MEDIATED' named entity '5.7' named entity 'DETERMINED' named entity 'STRUCTURES' named entity 'REPRESENT' named entity 'STATES' named entity 'POSITION' named entity 'ENGAGEMENT' named entity 'DETERMINED BY' named entity 'SURFACE' named entity 'SUBUNIT' named entity 'BINDING SITE' named entity 'CRYO-ELECTRON MICROSCOPY' named entity 'FUSION' named entity 'PROVIDES' named entity 'INTERMEDIATE' named entity 'CRYO-ELECTRON MICROSCOPY' named entity 'RECEPTOR BINDING' named entity 'DOMAIN' named entity 'GLYCOPROTEINS' named entity 'BINDING'

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