About: SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2

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About: SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2 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	SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2
Creator	Zhang, Yang Yin, Xin Carlin, Aaron Ward, Andrew Kevin, D Torres, Jonathan Garretson, Aaron Porell, Ryan Caradonna, Timothy Chanda, Summit Clausen, Thomas Corbett, Esko, Jeffrey Feldman, Jared Glass, Charles Godula, Kamil Golden, Gregory Gordts, Philip Hauser, Blake Jose, Joyce Kellman, Benjamin Laubach, Logan Leibel, Sandra Majowicz, Sydney Martino, Cameron Narayanan, Anoop Painter, Chelsea Pihl, Jessica Pu, Yuan Sandoval, Daniel Schmidt, Aaron Spliid, Charlotte Thacker, Bryan
Source	BioRxiv; Medline
abstract	We show that SARS-CoV-2 spike protein interacts with cell surface heparan sulfate and angiotensin converting enzyme 2 (ACE2) through its Receptor Binding Domain. Docking studies suggest a putative heparin/heparan sulfate-binding site adjacent to the domain that binds to ACE2. In vitro, binding of ACE2 and heparin to spike protein ectodomains occurs independently and a ternary complex can be generated using heparin as a template. Contrary to studies with purified components, spike protein binding to heparan sulfate and ACE2 on cells occurs codependently. Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus. These findings support a model for SARS-CoV-2 infection in which viral attachment and infection involves formation of a complex between heparan sulfate and ACE2. Manipulation of heparan sulfate or inhibition of viral adhesion by exogenous heparin may represent new therapeutic opportunities.
has issue date	2020-07-14(xsd:dateTime)
bibo:doi	10.1101/2020.07.14.201616
bibo:pmid	32699853
has license	biorxiv
sha1sum (hex)	c2d10ccd19f65b4f5e018b22bbf3dae1c963a77c
schema:url	https://doi.org/10.1101/2020.07.14.201616
resource representing a document's title	SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2
has PubMed identifier	32699853
schema:publication	bioRxiv
resource representing a document's body	covid:c2d10ccd19f65b4f5e018b22bbf3dae1c963a77c#body_text
is schema:about of	named entity 'viral' named entity 'spike' named entity 'generated' named entity 'ACE2' named entity 'attachment' named entity 'heparan sulfate' named entity 'ACE2' named entity 'Infection' named entity 'binding' named entity 'SARS-CoV-2' named entity 'protein' named entity 'heparin' named entity 'In vitro' named entity 'ACE2' named entity 'heparin' named entity 'heparin' named entity 'enzyme' named entity 'spike' named entity 'heparan sulfate' named entity 'SARS-CoV-2' named entity 'infection' named entity 'heparin' named entity 'ACE2' named entity 'spike protein' named entity 'lung' named entity 'ACE2' named entity 'heparan sulfate' named entity 'anticoagulant' named entity 'viral' named entity 'antiviral agent' named entity 'recombinant proteins' named entity 'hemagglutinin' named entity 'viral replication' named entity 'threonine' named entity 'rotavirus' named entity 'nucleocapsid' named entity 'mAb' named entity 'disaccharide' named entity 'Addgene' named entity 'protein' named entity 'infection' named entity 'culture medium' named entity 'disaccharide' named entity 'Thermo Fisher' named entity 'anticoagulant' named entity 'protein' named entity 'HEK293' named entity 'sulfation' named entity 'genetic studies' named entity 'culture medium'

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