About: Glycosaminoglycans induce conformational change in the SARS-CoV-2 Spike S1 Receptor Binding Domain

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About: Glycosaminoglycans induce conformational change in the SARS-CoV-2 Spike S1 Receptor Binding Domain 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	Glycosaminoglycans induce conformational change in the SARS-CoV-2 Spike S1 Receptor Binding Domain
Creator	Li, Yong Lima, Marcelo Skidmore, Mark Yates, Edwin Fernig, David Guerrini, Marco Miller, Gavin Mycroft-West, Courtney Turnbull, Jeremy Bisio, Antonella Elli, Stefano Forsyth, Nicholas Guimond, Scott Nunes, Quentin Procter, Patricia Rudd, Timothy Su, Dunhao
Source	BioRxiv
abstract	The glycosaminoglycan (GAG) class of polysaccharides are utilised by a plethora of microbial pathogens as receptors for adherence and invasion. The GAG heparin prevents infection by a range of viruses when added exogenously, including the S-associated coronavirus strain HSR1 and more recently we have demonstrated that heparin can block cellular invasion by SARS-CoV-2. Heparin has found widespread clinical use as anticoagulant drug and this molecule is routinely used as a proxy for the GAG, heparan sulphate (HS), a structural analogue located on the cell surface, which is a known receptor for viral invasion. Previous work has demonstrated that unfractionated heparin and low molecular weight heparins binds to the Spike (S1) protein receptor binding domain, inducing distinct conformational change and we have further explored the structural features of heparin with regard to these interactions. In this article, previous research is expanded to now include a broader range of GAG family members, including heparan sulphate. This research demonstrates that GAGs, other than those of heparin (or its derivatives), can also interact with the SARS-CoV-2 Spike S1 receptor binding domain and induce distinct conformational changes within this region. These findings pave the way for future research into next-generation, tailor-made, GAG-based antiviral agents, against SARS-CoV-2 and other members of the Coronaviridae.
has issue date	2020-04-29(xsd:dateTime)
bibo:doi	10.1101/2020.04.29.068767
has license	biorxiv
sha1sum (hex)	95359acf1d8a85c9eadb05b4769d3ba3178b4e45
schema:url	https://doi.org/10.1101/2020.04.29.068767
resource representing a document's title	Glycosaminoglycans induce conformational change in the SARS-CoV-2 Spike S1 Receptor Binding Domain
schema:publication	bioRxiv
resource representing a document's body	covid:95359acf1d8a85c9eadb05b4769d3ba3178b4e45#body_text
is schema:about of	named entity 'receptor' named entity 'article' named entity 'receptors' named entity 'GAGs' named entity 'MICROBIAL PATHOGENS' named entity 'UNFRACTIONATED HEPARIN' named entity 'TAILOR' named entity 'DISTINCT' named entity 'EXPANDED ' named entity 'RANGE' named entity 'FAMILY MEMBERS' named entity 'CORONAVIRUS' named entity 'WAY' named entity 'FOUND' named entity 'RECEPTOR BINDING' named entity 'Spike' named entity 'structural analogue' named entity 'heparin' named entity 'glycosaminoglycan' named entity 'coronavirus' named entity 'protein' named entity 'demonstrated' named entity 'conformational change' named entity 'members' named entity 'SARS-CoV-2' named entity 'receptor binding domain' named entity 'heparin' named entity 'antiviral agents' named entity 'coronavirus' named entity 'molecule' named entity 'anticoagulant drug' named entity 'viruses' named entity 'Receptor Binding Domain' named entity 'route of administration' named entity 'GAGs' named entity 'carbohydrates' named entity 'denaturing' named entity 'SARS-CoV-2' named entity 'LMWHs' named entity 'SARS-CoV-2' named entity 'conformational change' named entity 'protein' named entity 'SARS-CoV-2' named entity 'SARS-CoV-2' named entity 'inclusion bodies' named entity 'Recombinant protein' named entity 'flaviviruses' named entity 'ablate' named entity 'anticoagulant' named entity 'Germany' named entity 'toxicity' named entity 'broad-spectrum' named entity 'viral infection' named entity 'Lonza' named entity 'phosphate-buffered saline' named entity 'NaCl' named entity 'thrice' named entity 'Invitrogen' named entity 'pharmaceutical' named entity 'coronaviridae' named entity 'respiratory tract' named entity 'bioavailability' named entity 'SARS-CoV-2' named entity 'heparin' named entity 'expression vector' named entity 'coronavirus' named entity 'approved drugs' named entity 'GAGs'

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