Anti-SARS-CoV-2 activity of rhamnan sulfate from Monostroma nitidum

Authors
Song, Yuefan
He, Peng
Rodrigues, Andre L.
Datta, Payel
Tandon, Ritesh
Bates, John T.
Bierdeman, Michael A.
Chen, Chen
Dordick, Jonathan
Zhang, Fuming
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2021-12-01
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
Attribution 3.0 United States
CC 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.
Full Citation
Anti-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.
Abstract
The 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.
Description
Marine Drugs, 19, 685
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Multidisciplinary Digital Publishing Institute (MDPI)
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Marine Drugs
https://harc.rpi.edu/
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A full text version is available in DSpace@RPI
CC BY — Creative Commons Attribution