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Anti-SARS-CoV-2 Activity of Rhamnan Sulfate from Monostroma nitidum.
Song, Yuefan; He, Peng; Rodrigues, Andre L; Datta, Payel; Tandon, Ritesh; Bates, John T; Bierdeman, Michael A; Chen, Chen; Dordick, Jonathan; Zhang, Fuming; Linhardt, Robert J.
  • Song Y; Departments of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
  • He P; Departments of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
  • Rodrigues AL; Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
  • Datta P; Departments of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
  • Tandon R; Department of Microbiology and Immunology, University of Mississippi Medical Center, Jackson, MS 39216, USA.
  • Bates JT; Department of Medicine, University of Mississippi Medical Center, Jackson, MS 39216, USA.
  • Bierdeman MA; Department of Microbiology and Immunology, University of Mississippi Medical Center, Jackson, MS 39216, USA.
  • Chen C; Department of Medicine, University of Mississippi Medical Center, Jackson, MS 39216, USA.
  • Dordick J; Department of Medicine, University of Mississippi Medical Center, Jackson, MS 39216, USA.
  • Zhang F; Calroy Health Sciences, LLC., Scottsdale, AZ 85260, USA.
  • Linhardt RJ; Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Mar Drugs ; 19(12)2021 Nov 30.
Article in English | MEDLINE | ID: covidwho-1542656
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Antiviral Agents / Seaweed / Deoxy Sugars / Plant Extracts / SARS-CoV-2 / COVID-19 Drug Treatment / Mannans Type of study: Experimental Studies Topics: Variants Limits: Humans Language: English Journal subject: Biology / Pharmacology Year: 2021 Document Type: Article Affiliation country: Md19120685

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Antiviral Agents / Seaweed / Deoxy Sugars / Plant Extracts / SARS-CoV-2 / COVID-19 Drug Treatment / Mannans Type of study: Experimental Studies Topics: Variants Limits: Humans Language: English Journal subject: Biology / Pharmacology Year: 2021 Document Type: Article Affiliation country: Md19120685