http://socictopen.socict.org/files/original/b18d01d351ecc5600f8f74e249e3ce19.pdf ec0d016ce088e50184425f873521216d Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Coronavirus Description An account of the resource Dominio científico: Coronavirus Text A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text. Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Evidence of a putative glycosaminoglycan binding site on the glycosylated SARS-CoV-2 spike protein N-terminal domain. Creator An entity primarily responsible for making the resource Zachariah P. Schuurs, Edward Hammond, Timothy R. Rudd, Yassir A. Ahmed, Deirdre R. Coombe, Stefano Elli, Courtney J Mycroft-West, Marcelo A Lima, Mark A Skidmore, Richard Karlsson, Yen-Hsi Chen, Ieva Bagdonaite, Zhang Yang, Derek J Richard, Jeremy Turnbull, Vito Ferro, Neha S Gandhi Description An account of the resource SARS-CoV-2 has rapidly spread throughout the world's population since its initial discovery in 2019. The virus infects cells via a glycosylated spike protein located on its surface. The protein primarily binds to the angiotensin-converting enzyme-2 (ACE2) receptor, using glycosaminoglycans (GAGs) as co-receptors. Here, we performed bioinformatics and molecular dynamics simulations of the spike protein to investigate the existence of additional GAG binding sites on the receptor-binding domain (RBD), separate from previously reported heparin-binding sites. A putative GAG binding site in the N-terminal domain (NTD) of the protein was identified, encompassing residues 245-246. We hypothesized that GAGs of a sufficient length might bridge the gap between this site and the PRRARS furin cleavage site, including the mutation S247R. Docking studies using GlycoTorch Vina and subsequent MD simulations of the spike trimer in the presence of dodecasaccharides of the GAGs heparin and heparan sulfate supported this possibility. The heparan sulfate chain bridged the gap, binding the furin cleavage site and S247R. In contrast, the heparin chain bound the furin cleavage site and surrounding glycosylation structures, but not S247R. These findings identify a site in the spike protein that favors heparan sulfate binding that may be particularly pertinent for a better understanding of the recent UK and South African strains. This will also assist in future targeted therapy programs that could include repurposing clinical heparan sulfate mimetics. Date A point or period of time associated with an event in the lifecycle of the resource 2021 Subject The topic of the resource coronavirus, spike protein, covid-19, SARS-CoV-2, heparin, heparan sulfate, Cosolvent MD simulations Identifier An unambiguous reference to the resource within a given context 10.1016/j.csbj.2021.05.002 Source A related resource from which the described resource is derived Computational and structural biotechnology journal