About: Controlling the SARS-CoV-2 Spike Glycoprotein Conformation

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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
title	Controlling the SARS-CoV-2 Spike Glycoprotein Conformation
Creator	Haynes, Barton Edwards, Robert Borgnia, Mario Acharya, Priyamvada Gobeil, Sophie Henderson, Rory Hsu, Allen Janowska, Katarzyna Kopp, Megan Mansouri, Katayoun Parks, Rob Stalls, Victoria
source	BioRxiv; Medline; PMC
abstract	The coronavirus (CoV) viral host cell fusion spike (S) protein is the primary immunogenic target for virus neutralization and the current focus of many vaccine design efforts. The highly flexible S-protein, with its mobile domains, presents a moving target to the immune system. Here, to better understand S-protein mobility, we implemented a structure-based vector analysis of available β-CoV S-protein structures. We found that despite overall similarity in domain organization, different β-CoV strains display distinct S-protein configurations. Based on this analysis, we developed two soluble ectodomain constructs in which the highly immunogenic and mobile receptor binding domain (RBD) is locked in either the all-RBDs ‘down’ position or is induced to display a previously unobserved in SARS-CoV-2 2-RBDs ‘up’ configuration. These results demonstrate that the conformation of the S-protein can be controlled via rational design and provide a framework for the development of engineered coronavirus spike proteins for vaccine applications.
has issue date	2020-05-18(xsd:dateTime)
bibo:doi	10.1101/2020.05.18.102087
bibo:pmid	32511343
has license	cc-by-nc-nd
sha1sum (hex)	440b1938dfacddd6fc57f375a5c6986c5c7942ab
schema:url	https://doi.org/10.1101/2020.05.18.102087
resource representing a document's title	Controlling the SARS-CoV-2 Spike Glycoprotein Conformation
has PubMed Central identifier	PMC7252579
has PubMed identifier	32511343
schema:publication	bioRxiv
resource representing a document's body	covid:440b1938dfacddd6fc57f375a5c6986c5c7942ab#body_text
is schema:about of	named entity 'coronavirus' named entity 'highly' named entity 'rational design' named entity 'RBDs' named entity 'constructs' named entity 'structures' named entity 'similarity' named entity 'highly' named entity 'current' named entity 'mobility' named entity 'developed' named entity 'Here' named entity 'RBDs' named entity 'protein' named entity 'protein' named entity 'virus' named entity 'structure-based' named entity 'vaccine' named entity 'immunogenic' named entity 'protein structures' named entity 'spike (S) protein' named entity 'coronavirus' named entity 'receptor binding domain' named entity 'vector analysis' named entity 'β-CoV' named entity 'NSEM' named entity 'immunogen' named entity 'ectodomain' named entity 'dose was fractionated' named entity 'dihedral' named entity 'conformation' named entity 'cryo-EM' named entity 'PDB' named entity 'cysteine' named entity '1-up' named entity 'MERS' named entity 'receptor binding' named entity 'ectodomain' named entity 'NTD' named entity 'MERS' named entity 'mutagenesis' named entity 'NTD' named entity 'RBD' named entity 'OC43' named entity 'C-terminal' named entity 'protein structure' named entity 'trimerization' named entity 'β-sheet' named entity 'β-CoV' named entity 'rigid bodies' named entity 'transmembrane' named entity 'natural evolution' named entity 'GenBank' named entity 'vaccines' named entity 'protein' named entity 'NTD' named entity 'β-CoV' named entity 'supernatant' named entity 'SARS-CoV-2' named entity 'immunogen' named entity 'SARS' named entity 'immunogenicity' named entity 'SARS' named entity 'murine' named entity 'β-CoV' named entity 'RBD' named entity 'protein' named entity 'ethane' named entity 'dihedrals' named entity 'SARS-2'

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