SPR Sensor-Based Analysis of the Inhibition of Marine Sulfated Glycans on Interactions between Monkeypox Virus Proteins and Glycosaminoglycans
Sulfated glycans from marine organisms are excellent sources of naturally occurring glycosaminoglycan (GAG) mimetics that demonstrate therapeutic activities, such as antiviral/microbial infection, anticoagulant, anticancer, and anti-inflammation activities. Many viruses use the heparan sulfate (HS)...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-04-01
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| Series: | Marine Drugs |
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| Online Access: | https://www.mdpi.com/1660-3397/21/5/264 |
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| author | Peng He Deling Shi Yunran Li Ke Xia Seon Beom Kim Rohini Dwivedi Marwa Farrag Vitor H. Pomin Robert J. Linhardt Jonathan S. Dordick Fuming Zhang |
| author_facet | Peng He Deling Shi Yunran Li Ke Xia Seon Beom Kim Rohini Dwivedi Marwa Farrag Vitor H. Pomin Robert J. Linhardt Jonathan S. Dordick Fuming Zhang |
| author_sort | Peng He |
| collection | DOAJ |
| description | Sulfated glycans from marine organisms are excellent sources of naturally occurring glycosaminoglycan (GAG) mimetics that demonstrate therapeutic activities, such as antiviral/microbial infection, anticoagulant, anticancer, and anti-inflammation activities. Many viruses use the heparan sulfate (HS) GAG on the surface of host cells as co-receptors for attachment and initiating cell entry. Therefore, virion–HS interactions have been targeted to develop broad-spectrum antiviral therapeutics. Here we report the potential anti-monkeypox virus (MPXV) activities of eight defined marine sulfated glycans, three fucosylated chondroitin sulfates, and three sulfated fucans extracted from the sea cucumber species <i>Isostichopus badionotus</i>, <i>Holothuria floridana</i>, and <i>Pentacta pygmaea</i>, and the sea urchin <i>Lytechinus variegatus</i>, as well as two chemically desulfated derivatives. The inhibitions of these marine sulfated glycans on MPXV A29 and A35 protein–heparin interactions were evaluated using surface plasmon resonance (SPR). These results demonstrated that the viral surface proteins of MPXV A29 and A35 bound to heparin, which is a highly sulfated HS, and sulfated glycans from sea cucumbers showed strong inhibition of MPXV A29 and A35 interactions. The study of molecular interactions between viral proteins and host cell GAGs is important in developing therapeutics for the prevention and treatment of MPXV. |
| first_indexed | 2024-03-11T03:33:10Z |
| format | Article |
| id | doaj.art-32ebff160fb446768fcc7b9f7d09654c |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-03-11T03:33:10Z |
| publishDate | 2023-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-32ebff160fb446768fcc7b9f7d09654c2023-11-18T02:12:33ZengMDPI AGMarine Drugs1660-33972023-04-0121526410.3390/md21050264SPR Sensor-Based Analysis of the Inhibition of Marine Sulfated Glycans on Interactions between Monkeypox Virus Proteins and GlycosaminoglycansPeng He0Deling Shi1Yunran Li2Ke Xia3Seon Beom Kim4Rohini Dwivedi5Marwa Farrag6Vitor H. Pomin7Robert J. Linhardt8Jonathan S. Dordick9Fuming Zhang10Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USACenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USACenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USACenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USADepartment of BioMolecular Sciences, Research Institute of Pharmaceutical Sciences, The University of Mississippi, Oxford, MS 38677, USADepartment of BioMolecular Sciences, Research Institute of Pharmaceutical Sciences, The University of Mississippi, Oxford, MS 38677, USADepartment of BioMolecular Sciences, Research Institute of Pharmaceutical Sciences, The University of Mississippi, Oxford, MS 38677, USADepartment of BioMolecular Sciences, Research Institute of Pharmaceutical Sciences, The University of Mississippi, Oxford, MS 38677, USACenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USACenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USACenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USASulfated glycans from marine organisms are excellent sources of naturally occurring glycosaminoglycan (GAG) mimetics that demonstrate therapeutic activities, such as antiviral/microbial infection, anticoagulant, anticancer, and anti-inflammation activities. Many viruses use the heparan sulfate (HS) GAG on the surface of host cells as co-receptors for attachment and initiating cell entry. Therefore, virion–HS interactions have been targeted to develop broad-spectrum antiviral therapeutics. Here we report the potential anti-monkeypox virus (MPXV) activities of eight defined marine sulfated glycans, three fucosylated chondroitin sulfates, and three sulfated fucans extracted from the sea cucumber species <i>Isostichopus badionotus</i>, <i>Holothuria floridana</i>, and <i>Pentacta pygmaea</i>, and the sea urchin <i>Lytechinus variegatus</i>, as well as two chemically desulfated derivatives. The inhibitions of these marine sulfated glycans on MPXV A29 and A35 protein–heparin interactions were evaluated using surface plasmon resonance (SPR). These results demonstrated that the viral surface proteins of MPXV A29 and A35 bound to heparin, which is a highly sulfated HS, and sulfated glycans from sea cucumbers showed strong inhibition of MPXV A29 and A35 interactions. The study of molecular interactions between viral proteins and host cell GAGs is important in developing therapeutics for the prevention and treatment of MPXV.https://www.mdpi.com/1660-3397/21/5/264monkeypox virusprotein A29protein A35heparinsea cucumbersmarine sulfated glycans |
| spellingShingle | Peng He Deling Shi Yunran Li Ke Xia Seon Beom Kim Rohini Dwivedi Marwa Farrag Vitor H. Pomin Robert J. Linhardt Jonathan S. Dordick Fuming Zhang SPR Sensor-Based Analysis of the Inhibition of Marine Sulfated Glycans on Interactions between Monkeypox Virus Proteins and Glycosaminoglycans Marine Drugs monkeypox virus protein A29 protein A35 heparin sea cucumbers marine sulfated glycans |
| title | SPR Sensor-Based Analysis of the Inhibition of Marine Sulfated Glycans on Interactions between Monkeypox Virus Proteins and Glycosaminoglycans |
| title_full | SPR Sensor-Based Analysis of the Inhibition of Marine Sulfated Glycans on Interactions between Monkeypox Virus Proteins and Glycosaminoglycans |
| title_fullStr | SPR Sensor-Based Analysis of the Inhibition of Marine Sulfated Glycans on Interactions between Monkeypox Virus Proteins and Glycosaminoglycans |
| title_full_unstemmed | SPR Sensor-Based Analysis of the Inhibition of Marine Sulfated Glycans on Interactions between Monkeypox Virus Proteins and Glycosaminoglycans |
| title_short | SPR Sensor-Based Analysis of the Inhibition of Marine Sulfated Glycans on Interactions between Monkeypox Virus Proteins and Glycosaminoglycans |
| title_sort | spr sensor based analysis of the inhibition of marine sulfated glycans on interactions between monkeypox virus proteins and glycosaminoglycans |
| topic | monkeypox virus protein A29 protein A35 heparin sea cucumbers marine sulfated glycans |
| url | https://www.mdpi.com/1660-3397/21/5/264 |
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