About: A thermostable, closed, SARS-CoV-2 spike protein trimer

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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	A thermostable, closed, SARS-CoV-2 spike protein trimer
Creator	Goodfellow, Ian Zhang, Ying Hosmillo, Myra Baker, Stephen Xiong, Xiaoli Ke, Zunlong James, Leo Briggs, John Bergamaschi, Laura Carter, Andrew Ciazynska, Katarzyna Nathan, James Qu, Kun Scheres, Sjors Baxendale, Helen Doffinger, Rainer Ebrahimi, Soraya Grice, Guinevere
Source	BioRxiv
abstract	The spike (S) protein of SARS-CoV-2 mediates receptor binding and cell entry and is the dominant target of the immune system. S exhibits substantial conformational flexibility. It transitions from closed to open conformations to expose its receptor binding site, and subsequently from prefusion to postfusion conformations to mediate fusion of viral and cellular membranes. S protein derivatives are components of vaccine candidates and diagnostic assays, as well as tools for research into the biology and immunology of SARS-CoV-2. Here we have designed mutations in S which allow production of thermostable, crosslinked, S protein trimers that are trapped in the closed, pre-fusion, state. We have determined the structures of crosslinked and non-crosslinked proteins, identifying two distinct closed conformations of the S trimer. We demonstrate that the designed, thermostable, closed S trimer can be used in serological assays. This protein has potential applications as a reagent for serology, virology and as an immunogen.
has issue date	2020-06-17(xsd:dateTime)
bibo:doi	10.1101/2020.06.15.152835
has license	biorxiv
sha1sum (hex)	34f30726b9bc493be2c0aa03ccc269b73bd6592c
schema:url	https://doi.org/10.1101/2020.06.15.152835
resource representing a document's title	A thermostable, closed, SARS-CoV-2 spike protein trimer
schema:publication	bioRxiv
resource representing a document's body	covid:34f30726b9bc493be2c0aa03ccc269b73bd6592c#body_text
is schema:about of	named entity 'dominant' named entity 'cellular membranes' named entity 'protein' named entity 'thermostable' named entity 'SARS-CoV-2' named entity 'expose' named entity 'mutations' named entity 'fusion' named entity 'conformational' named entity 'cell' named entity 'assays' named entity 'serological' named entity 'tools' named entity 'SARS-CoV-2' named entity 'receptor' named entity 'immune system' named entity 'production' named entity 'SARS-CoV-2' named entity 'protein' named entity 'protein' named entity 'SARS-CoV-2' named entity 'middle east respiratory syndrome' named entity 'binding site' named entity 'phenylmethylsulfonyl fluoride' named entity 'IgG' named entity 'postfusion' named entity 'trimers' named entity '36 hours' named entity 'protein production' named entity 'micelles' named entity 'SARS-CoV-2' named entity 'serological' named entity 'GP160' named entity 'RPH' named entity 'wild type' named entity 'immune response' named entity 'immunogens' named entity 'crosslinked' named entity 'trimers' named entity 'antibody' named entity 'crosslinked' named entity 'immunisation' named entity 'protein' named entity 'trimers' named entity 'Tween 20' named entity 'binding region' named entity 'SARS-CoV-1' named entity 'receptor binding' named entity 'reducing conditions' named entity 'RBD' named entity 'antibody' named entity 'supernatant' named entity 'binding site' named entity 'SARS-CoV-2' named entity 'IgG' named entity 'East of England' named entity 'detergent' named entity 'RBD' named entity 'beta-mercaptoethanol' named entity 'Luminex' named entity 'SARS-CoV-1' named entity 'postfusion' named entity 'closed conformation' named entity 'proline' named entity 'protein' named entity 'crosslink' named entity 'protein'

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