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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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Autores principales: He, Peng, Shi, Deling, Li, Yunran, Xia, Ke, Kim, Seon Beom, Dwivedi, Rohini, Farrag, Marwa, Pomin, Vitor H., Linhardt, Robert J., Dordick, Jonathan S., Zhang, Fuming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10222398/
https://www.ncbi.nlm.nih.gov/pubmed/37233458
http://dx.doi.org/10.3390/md21050264
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author He, Peng
Shi, Deling
Li, Yunran
Xia, Ke
Kim, Seon Beom
Dwivedi, Rohini
Farrag, Marwa
Pomin, Vitor H.
Linhardt, Robert J.
Dordick, Jonathan S.
Zhang, Fuming
author_facet He, Peng
Shi, Deling
Li, Yunran
Xia, Ke
Kim, Seon Beom
Dwivedi, Rohini
Farrag, Marwa
Pomin, Vitor H.
Linhardt, Robert J.
Dordick, Jonathan S.
Zhang, Fuming
author_sort He, Peng
collection PubMed
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 Isostichopus badionotus, Holothuria floridana, and Pentacta pygmaea, and the sea urchin Lytechinus variegatus, 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.
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spelling pubmed-102223982023-05-28 SPR Sensor-Based Analysis of the Inhibition of Marine Sulfated Glycans on Interactions between Monkeypox Virus Proteins and Glycosaminoglycans He, Peng Shi, Deling Li, Yunran Xia, Ke Kim, Seon Beom Dwivedi, Rohini Farrag, Marwa Pomin, Vitor H. Linhardt, Robert J. Dordick, Jonathan S. Zhang, Fuming Mar Drugs Article 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 Isostichopus badionotus, Holothuria floridana, and Pentacta pygmaea, and the sea urchin Lytechinus variegatus, 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. MDPI 2023-04-25 /pmc/articles/PMC10222398/ /pubmed/37233458 http://dx.doi.org/10.3390/md21050264 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
He, Peng
Shi, Deling
Li, Yunran
Xia, Ke
Kim, Seon Beom
Dwivedi, Rohini
Farrag, Marwa
Pomin, Vitor H.
Linhardt, Robert J.
Dordick, Jonathan S.
Zhang, Fuming
SPR Sensor-Based Analysis of the Inhibition of Marine Sulfated Glycans on Interactions between Monkeypox Virus Proteins and Glycosaminoglycans
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 Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10222398/
https://www.ncbi.nlm.nih.gov/pubmed/37233458
http://dx.doi.org/10.3390/md21050264
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