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dc.rights.licenseCC BY — Creative Commons Attribution
dc.contributor.authorSong, Yuefan
dc.contributor.authorHe, Peng
dc.contributor.authorRodrigues, Andre L.
dc.contributor.authorDatta, Payel
dc.contributor.authorTandon, Ritesh
dc.contributor.authorBates, John T.
dc.contributor.authorBierdeman, Michael A.
dc.contributor.authorChen, Chen
dc.contributor.authorDordick, Jonathan
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.date2021
dc.date.accessioned2022-06-21T13:59:46Z
dc.date.available2022-06-21T13:59:46Z
dc.date.issued2021-12-01
dc.identifier.citationAnti-SARS-CoV-2 activity of rhamnan sulfate from Monostroma nitidum, Y. Song, P. He, A. L. Rodrigues, P. Datta, R. Tandon, J. T. Bates, M. Bierdeman, C. Chen, J. S. Dordick, F. Zhang, R. J. Linhardt, Marine Drugs, 19, 685, 2021.
dc.identifier.issn16603397
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5044
dc.identifier.urihttps://doi.org/10.3390/md19120685
dc.descriptionMarine Drugs, 19, 685
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractThe COVID-19 pandemic is a major human health concern. The pathogen responsible for COVID-19, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), invades its host through the interaction of its spike (S) protein with a host cell receptor, angiotensin-converting enzyme 2 (ACE2). In addition to ACE2, heparan sulfate (HS) on the surface of host cells also plays a significant role as a co-receptor. Our previous studies demonstrated that sulfated glycans, such as heparin and fucoidans, show anti-COVID-19 activities. In the current study, rhamnan sulfate (RS), a polysaccharide with a rhamnose backbone from a green seaweed, Monostroma nitidum, was evaluated for binding to the S-protein from SARS-CoV-2 and inhibition of viral infectivity in vitro. The structural characteristics of RS were investigated by determining its monosaccharide composition and performing two-dimensional nuclear magnetic resonance. RS inhibition of the interaction of heparin, a highly sulfated HS, with the SARS-CoV-2 spike protein (from wild type and different mutant variants) was studied using surface plasmon resonance (SPR). In competitive binding studies, the IC50 of RS against the S-protein receptor binding domain (RBD) binding to immobilized heparin was 1.6 ng/mL, which is much lower than the IC50 for heparin (~750 ng/mL). RS showed stronger inhibition than heparin on the S-protein RBD or pseudoviral particles binding to immobilized heparin. Finally, in an in vitro cell-based assay, RS showed strong antiviral activities against wild type SARS-CoV-2 and the delta variant.
dc.description.sponsorshipNational Science Foundation
dc.languageen_US
dc.language.isoENG
dc.publisherMultidisciplinary Digital Publishing Institute (MDPI)
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofMarine Drugs
dc.relation.urihttps://harc.rpi.edu/
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleAnti-SARS-CoV-2 activity of rhamnan sulfate from Monostroma nitidumen_US
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.accessRightsOpen Access
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.3390/md19120685
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.volume19


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CC BY — Creative Commons Attribution
Except where otherwise noted, this item's license is described as CC BY — Creative Commons Attribution