About: Characterization of heparin and severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) spike glycoprotein binding interactions

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About: Characterization of heparin and severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) spike glycoprotein binding interactions Goto Sponge NotDistinct Permalink

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Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Characterization of heparin and severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) spike glycoprotein binding interactions
Creator	Fu, Li Montgomery, David Kim, So Woods, Robert Zhang, R Kim, S Fu, M Grant, D Dordick, Jonathan Fuster, Mark Grant, Oliver Jin, Weihua Linhardt, Robert Linhardt, F Montgomery, A Sood, Amika Sood, W Woods, J Zhang, Fuming
Source	Elsevier; Medline; PMC
abstract	Severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) has resulted in a pandemic and continues to spread around the globe at an unprecedented rate. To date, no effective therapeutic is available to fight its associated disease, COVID-19. Our discovery of a novel insertion of glycosaminoglycan (GAG)-binding motif at S1/S2 proteolytic cleavage site (681–686 (PRRARS)) and two other GAG-binding-like motifs within SARS-CoV-2 spike glycoprotein (SGP) led us to hypothesize that host cell surface GAGs may interact SARS-CoV-2 SGPs to facilitate host cell entry. Using a surface plasmon resonance direct binding assay, we found that both monomeric and trimeric SARS-CoV-2 SGP bind more tightly to immobilized heparin (K(D) = 40 pM and 73 pM, respectively) than the SARS-CoV and MERS-CoV SGPs (500 nM and 1 nM, respectively). In competitive binding studies, the IC(50) of heparin, tri-sulfated non-anticoagulant heparan sulfate, and non-anticoagulant low molecular weight heparin against SARS-CoV-2 SGP binding to immobilized heparin were 0.056 μM, 0.12 μM, and 26.4 μM, respectively. Finally, unbiased computational ligand docking indicates that heparan sulfate interacts with the GAG-binding motif at the S1/S2 site on each monomer interface in the trimeric SARS-CoV-2 SGP, and at another site (453–459 (YRLFRKS)) when the receptor-binding domain is in an open conformation. The current study serves a foundation to further investigate biological roles of GAGs in SARS-CoV-2 pathogenesis. Furthermore, our findings may provide additional basis for further heparin-based interventions for COVID-19 patients exhibiting thrombotic complications.
has issue date	2020-07-10(xsd:dateTime)
bibo:doi	10.1016/j.antiviral.2020.104873
bibo:pmid	32653452
has license	no-cc
sha1sum (hex)	35781961b5403c1acd147fd090ce91fce369729a
schema:url	https://doi.org/10.1016/j.antiviral.2020.104873
resource representing a document's title	Characterization of heparin and severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) spike glycoprotein binding interactions
has PubMed Central identifier	PMC7347485
has PubMed identifier	32653452
schema:publication	Antiviral Res
resource representing a document's body	covid:35781961b5403c1acd147fd090ce91fce369729a#body_text
is schema:about of	named entity 'severe acute respiratory syndrome-related coronavirus' named entity 'coronavirus' named entity 'interactions' named entity 'interactions' named entity 'Antiviral' named entity 'heparin' named entity 'glycoprotein' named entity 'severe acute respiratory syndrome-related coronavirus' named entity 'glycoprotein' named entity 'heparin' named entity 'Middle East respiratory syndrome-related coronavirus' named entity 'COVID-19' named entity 'SARS-CoV-2' named entity 'standard deviations' named entity 'RBD' named entity 'RBD' named entity 'oxidation' named entity 'conformational change' named entity 'SARS-CoV' named entity 'SARS-CoV-2' named entity 'RBD' named entity 'high affinity' named entity 'nucleocapsid protein' named entity 'human lung' named entity 'streptavidin' named entity 'amine' named entity 'venous thromboembolism' named entity 'competitive inhibitors' named entity 'binding affinity' named entity 'COVID' named entity 'Monomeric' named entity 'anticoagulant' named entity 'SARS-CoV' named entity 'desulfated' named entity 'fibroblast growth factor 2' named entity 'glycans' named entity 'SGP' named entity 'cell entry' named entity 'SGP' named entity 'dose response' named entity 'MERS-CoV' named entity 'sulfation' named entity 'SARS-CoV' named entity 'SARS-CoV-2' named entity 'sulfate' named entity 'GAGs' named entity 'Virion' named entity 'coronavirus disease 2019' named entity 'fractionation' named entity 'cell entry' named entity 'homology modeling' named entity 'equilibrium dissociation constant' named entity 'open conformation' named entity '4.01' named entity 'arginine' named entity 'GAGs' named entity 'integrin' named entity 'binding motif' named entity 'sulfates' named entity 'dipeptidyl peptidase 4' named entity 'SARS-CoV-2' named entity 'SARS-CoV-2' named entity 'transmembrane serine protease 2'

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