Sulfated Glycans Inhibit the Interaction of MERS-CoV Receptor Binding Domain with Heparin
Middle East respiratory syndrome coronavirus (MERS-CoV) is a zoonotic virus with high contagion and mortality rates. Heparan sulfate proteoglycans (HSPGs) are ubiquitously expressed on the surface of mammalian cells. Owing to its high negatively charged property, heparan sulfate (HS) on the surface...
| Main Authors: | , , , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-02-01
|
| Series: | Viruses |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1999-4915/16/2/237 |
| _version_ | 1797296824240832512 |
|---|---|
| author | Jiyuan Yang Yuefan Song Weihua Jin Ke Xia Grace C. Burnett Wanjin Qiao John T. Bates Vitor H. Pomin Chunyu Wang Mingqiang Qiao Robert J. Linhardt Jonathan S. Dordick Fuming Zhang |
| author_facet | Jiyuan Yang Yuefan Song Weihua Jin Ke Xia Grace C. Burnett Wanjin Qiao John T. Bates Vitor H. Pomin Chunyu Wang Mingqiang Qiao Robert J. Linhardt Jonathan S. Dordick Fuming Zhang |
| author_sort | Jiyuan Yang |
| collection | DOAJ |
| description | Middle East respiratory syndrome coronavirus (MERS-CoV) is a zoonotic virus with high contagion and mortality rates. Heparan sulfate proteoglycans (HSPGs) are ubiquitously expressed on the surface of mammalian cells. Owing to its high negatively charged property, heparan sulfate (HS) on the surface of host cells is used by many viruses as cofactor to facilitate viral attachment and initiate cellular entry. Therefore, inhibition of the interaction between viruses and HS could be a promising target to inhibit viral infection. In the current study, the interaction between the receptor-binding domain (RBD) of MERS-CoV and heparin was exploited to assess the inhibitory activity of various sulfated glycans such as glycosaminoglycans, marine-sourced glycans (sulfated fucans, fucosylated chondroitin sulfates, fucoidans, and rhamnan sulfate), pentosan polysulfate, and mucopolysaccharide using Surface Plasmon Resonance. We believe this study provides valuable insights for the development of sulfated glycan-based inhibitors as potential antiviral agents. |
| first_indexed | 2024-03-07T22:11:17Z |
| format | Article |
| id | doaj.art-a85e0c11f5ad435dbfcfef4089272a77 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-07T22:11:17Z |
| publishDate | 2024-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-a85e0c11f5ad435dbfcfef4089272a772024-02-23T15:37:34ZengMDPI AGViruses1999-49152024-02-0116223710.3390/v16020237Sulfated Glycans Inhibit the Interaction of MERS-CoV Receptor Binding Domain with HeparinJiyuan Yang0Yuefan Song1Weihua Jin2Ke Xia3Grace C. Burnett4Wanjin Qiao5John T. Bates6Vitor H. Pomin7Chunyu Wang8Mingqiang Qiao9Robert J. Linhardt10Jonathan S. Dordick11Fuming Zhang12The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, ChinaDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USACollege of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou 310014, ChinaDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USADepartment of Cell & Molecular Biology, The University of Mississippi Medical Center, Jackson, MS 39216, USAThe Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, ChinaDepartment of Cell & Molecular Biology, The University of Mississippi Medical Center, Jackson, MS 39216, USADepartment of BioMolecular Sciences, Research Institute of Pharmaceutical Sciences, The University of Mississippi, Oxford, MS 38677, USADepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USAThe Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, ChinaDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USADepartments of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, USADepartments of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, USAMiddle East respiratory syndrome coronavirus (MERS-CoV) is a zoonotic virus with high contagion and mortality rates. Heparan sulfate proteoglycans (HSPGs) are ubiquitously expressed on the surface of mammalian cells. Owing to its high negatively charged property, heparan sulfate (HS) on the surface of host cells is used by many viruses as cofactor to facilitate viral attachment and initiate cellular entry. Therefore, inhibition of the interaction between viruses and HS could be a promising target to inhibit viral infection. In the current study, the interaction between the receptor-binding domain (RBD) of MERS-CoV and heparin was exploited to assess the inhibitory activity of various sulfated glycans such as glycosaminoglycans, marine-sourced glycans (sulfated fucans, fucosylated chondroitin sulfates, fucoidans, and rhamnan sulfate), pentosan polysulfate, and mucopolysaccharide using Surface Plasmon Resonance. We believe this study provides valuable insights for the development of sulfated glycan-based inhibitors as potential antiviral agents.https://www.mdpi.com/1999-4915/16/2/237HSPGsheparinMERS-CoVsulfated glycanssurface plasmon resonance |
| spellingShingle | Jiyuan Yang Yuefan Song Weihua Jin Ke Xia Grace C. Burnett Wanjin Qiao John T. Bates Vitor H. Pomin Chunyu Wang Mingqiang Qiao Robert J. Linhardt Jonathan S. Dordick Fuming Zhang Sulfated Glycans Inhibit the Interaction of MERS-CoV Receptor Binding Domain with Heparin Viruses HSPGs heparin MERS-CoV sulfated glycans surface plasmon resonance |
| title | Sulfated Glycans Inhibit the Interaction of MERS-CoV Receptor Binding Domain with Heparin |
| title_full | Sulfated Glycans Inhibit the Interaction of MERS-CoV Receptor Binding Domain with Heparin |
| title_fullStr | Sulfated Glycans Inhibit the Interaction of MERS-CoV Receptor Binding Domain with Heparin |
| title_full_unstemmed | Sulfated Glycans Inhibit the Interaction of MERS-CoV Receptor Binding Domain with Heparin |
| title_short | Sulfated Glycans Inhibit the Interaction of MERS-CoV Receptor Binding Domain with Heparin |
| title_sort | sulfated glycans inhibit the interaction of mers cov receptor binding domain with heparin |
| topic | HSPGs heparin MERS-CoV sulfated glycans surface plasmon resonance |
| url | https://www.mdpi.com/1999-4915/16/2/237 |
| work_keys_str_mv | AT jiyuanyang sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT yuefansong sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT weihuajin sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT kexia sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT gracecburnett sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT wanjinqiao sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT johntbates sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT vitorhpomin sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT chunyuwang sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT mingqiangqiao sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT robertjlinhardt sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT jonathansdordick sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin AT fumingzhang sulfatedglycansinhibittheinteractionofmerscovreceptorbindingdomainwithheparin |