Kinetic and Structural Aspects of Glycosaminoglycan–Monkeypox Virus Protein A29 Interactions Using Surface Plasmon Resonance
Monkeypox virus (MPXV), a member of the Orthopoxvirus genus, has begun to spread into many countries worldwide. While the prevalence of monkeypox in Central and Western Africa is well-known, the recent rise in the number of cases spread through intimate personal contact, particularly in the United S...
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MDPI AG
2022-09-01
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author | Deling Shi Peng He Yuefan Song Shuihong Cheng Robert J. Linhardt Jonathan S. Dordick Lianli Chi Fuming Zhang |
author_facet | Deling Shi Peng He Yuefan Song Shuihong Cheng Robert J. Linhardt Jonathan S. Dordick Lianli Chi Fuming Zhang |
author_sort | Deling Shi |
collection | DOAJ |
description | Monkeypox virus (MPXV), a member of the Orthopoxvirus genus, has begun to spread into many countries worldwide. While the prevalence of monkeypox in Central and Western Africa is well-known, the recent rise in the number of cases spread through intimate personal contact, particularly in the United States, poses a grave international threat. Previous studies have shown that cell-surface heparan sulfate (HS) is important for vaccinia virus (VACV) infection, particularly the binding of VACV A27, which appears to mediate the binding of virus to cellular HS. Some other glycosaminoglycans (GAGs) also bind to proteins on Orthopoxviruses. In this study, by using surface plasmon resonance, we demonstrated that MPXV A29 protein (a homolog of VACV A27) binds to GAGs including heparin and chondroitin sulfate/dermatan sulfate. The negative charges on GAGs are important for GAG–MPXV A29 interaction. GAG analogs, pentosan polysulfate and mucopolysaccharide polysulfate, show strong inhibition of MPXV A29–heparin interaction. A detailed understanding on the molecular interactions involved in this disease should accelerate the development of therapeutics and drugs for the treatment of MPXV. |
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language | English |
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spelling | doaj.art-d3a1ab7581164d71b1db04830514f8d32023-11-23T18:00:48ZengMDPI AGMolecules1420-30492022-09-012718589810.3390/molecules27185898Kinetic and Structural Aspects of Glycosaminoglycan–Monkeypox Virus Protein A29 Interactions Using Surface Plasmon ResonanceDeling Shi0Peng He1Yuefan Song2Shuihong Cheng3Robert J. Linhardt4Jonathan S. Dordick5Lianli Chi6Fuming Zhang7National Glycoengineering Research Center, Shandong University, Qingdao 266237, ChinaCenter 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, USACenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USANational Glycoengineering Research Center, Shandong University, Qingdao 266237, ChinaCenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USAMonkeypox virus (MPXV), a member of the Orthopoxvirus genus, has begun to spread into many countries worldwide. While the prevalence of monkeypox in Central and Western Africa is well-known, the recent rise in the number of cases spread through intimate personal contact, particularly in the United States, poses a grave international threat. Previous studies have shown that cell-surface heparan sulfate (HS) is important for vaccinia virus (VACV) infection, particularly the binding of VACV A27, which appears to mediate the binding of virus to cellular HS. Some other glycosaminoglycans (GAGs) also bind to proteins on Orthopoxviruses. In this study, by using surface plasmon resonance, we demonstrated that MPXV A29 protein (a homolog of VACV A27) binds to GAGs including heparin and chondroitin sulfate/dermatan sulfate. The negative charges on GAGs are important for GAG–MPXV A29 interaction. GAG analogs, pentosan polysulfate and mucopolysaccharide polysulfate, show strong inhibition of MPXV A29–heparin interaction. A detailed understanding on the molecular interactions involved in this disease should accelerate the development of therapeutics and drugs for the treatment of MPXV.https://www.mdpi.com/1420-3049/27/18/5898A29chondroitin sulfatedermatan sulfateheparinmonkeypox virussurface plasmon resonance |
spellingShingle | Deling Shi Peng He Yuefan Song Shuihong Cheng Robert J. Linhardt Jonathan S. Dordick Lianli Chi Fuming Zhang Kinetic and Structural Aspects of Glycosaminoglycan–Monkeypox Virus Protein A29 Interactions Using Surface Plasmon Resonance Molecules A29 chondroitin sulfate dermatan sulfate heparin monkeypox virus surface plasmon resonance |
title | Kinetic and Structural Aspects of Glycosaminoglycan–Monkeypox Virus Protein A29 Interactions Using Surface Plasmon Resonance |
title_full | Kinetic and Structural Aspects of Glycosaminoglycan–Monkeypox Virus Protein A29 Interactions Using Surface Plasmon Resonance |
title_fullStr | Kinetic and Structural Aspects of Glycosaminoglycan–Monkeypox Virus Protein A29 Interactions Using Surface Plasmon Resonance |
title_full_unstemmed | Kinetic and Structural Aspects of Glycosaminoglycan–Monkeypox Virus Protein A29 Interactions Using Surface Plasmon Resonance |
title_short | Kinetic and Structural Aspects of Glycosaminoglycan–Monkeypox Virus Protein A29 Interactions Using Surface Plasmon Resonance |
title_sort | kinetic and structural aspects of glycosaminoglycan monkeypox virus protein a29 interactions using surface plasmon resonance |
topic | A29 chondroitin sulfate dermatan sulfate heparin monkeypox virus surface plasmon resonance |
url | https://www.mdpi.com/1420-3049/27/18/5898 |
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