About: Structures, conformations and distributions of SARS-CoV-2 spike protein trimers on intact virions

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About: Structures, conformations and distributions of SARS-CoV-2 spike protein trimers on intact virions Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structures, conformations and distributions of SARS-CoV-2 spike protein trimers on intact virions
Creator	Bartenschlager, Ralf Xiong, Xiaoli Cortese, Mirko Kräusslich, Hans-Georg Ke, Zunlong Neufeldt, Christopher Briggs, John Lu, John Mckeane, Lesley Nakane, Takanori Oton, Joaquin Peukes, Julia Qu, Kun Scheres, Sjors Zila, Vojtech Zivanov, Jasenko
Source	BioRxiv
abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude. Heavily glycosylated S trimers bind the ACE2 receptor and mediate entry of virions into target cells. S exhibits extensive conformational flexibility: it modulates the exposure of its receptor binding site and later undergoes complete structural rearrangement to drive fusion of viral and cellular membranes. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy. The structure and distribution of S on the virion surface, however, has not been characterised. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions, determining the high-resolution structure, conformational flexibility and distributions of S trimers in situ on the virion surface. These results provide a basis for understanding the conformations of S present on the virion, and for studying their interactions with neutralizing antibodies.
has issue date	2020-06-27(xsd:dateTime)
bibo:doi	10.1101/2020.06.27.174979
has license	biorxiv
sha1sum (hex)	cbc74c84b92cbc677ecdabc5f7f88a522f1c3fce
schema:url	https://doi.org/10.1101/2020.06.27.174979
resource representing a document's title	Structures, conformations and distributions of SARS-CoV-2 spike protein trimers on intact virions
schema:publication	bioRxiv
resource representing a document's body	covid:cbc74c84b92cbc677ecdabc5f7f88a522f1c3fce#body_text
is schema:about of	named entity 'cryo-electron microscopy' named entity 'proteins' named entity 'virion' named entity 'structure' named entity 'provide' named entity 'STRUCTURE' named entity 'VIRIONS' named entity 'PROVIDE' named entity 'RESULTS' named entity 'SPIKE PROTEIN' named entity 'DISTRIBUTIONS' named entity 'conformations' named entity 'basis' named entity 'virion' named entity 'Here' named entity 'Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)' named entity 'bind' named entity 'target cells' named entity 'structural' named entity 'virions' named entity 'cryo-electron microscopy' named entity 'glycosylated' named entity 'lipid bilayer' named entity 'virion' named entity 'ACE2 receptor' named entity 'N-glycosylation sites' named entity 'supernatants' named entity 'salt bridge' named entity 'virions' named entity 'N-terminal domain' named entity 'data set' named entity 'Virions' named entity 'PBS' named entity 'protein' named entity 'Germany' named entity 'lipids' named entity 'Beckman Coulter Life Sciences' named entity 'S1C' named entity 'RBD' named entity 'electron tomography' named entity 'RNA' named entity 'Euler angles' named entity 'trimers' named entity 'trimers' named entity 'PBS' named entity 'Göttingen' named entity 'postfusion' named entity 'conformation' named entity 'Gels' named entity 'infection' named entity 'amplicon' named entity '4.3' named entity 'NTD' named entity 'SARS-CoV-2' named entity 'data acquisition' named entity 'NTD' named entity 'spike protein' named entity 'lipid envelope' named entity 'virus' named entity 'human lung' named entity 'betacoronavirus' named entity 'molecular models' named entity 'protein' named entity 'protein' named entity 'Total protein' named entity 'image processing' named entity 'rotamer' named entity 'glycans' named entity '7.2'

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