Conformational Dynamics of Nonenveloped Circovirus Capsid to the Host Cell Receptor
Summary: Circovirus, comprising one capsid protein, is the smallest nonenveloped virus and induces lymphopenia. Circovirus can be used to explore the cell adhesion mechanism of nonenveloped viruses. We developed a single-molecule fluorescence resonance energy transfer (smFRET) assay to directly visu...
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| Format: | Article |
| Language: | English |
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Elsevier
2020-10-01
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| Series: | iScience |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004220307392 |
| _version_ | 1818881972477362176 |
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| author | Jiarong Li Jinyan Gu Cui Lin Jianwei Zhou Shengnan Wang Jin Lei Fengcai Wen Bo Sun Jiyong Zhou |
| author_facet | Jiarong Li Jinyan Gu Cui Lin Jianwei Zhou Shengnan Wang Jin Lei Fengcai Wen Bo Sun Jiyong Zhou |
| author_sort | Jiarong Li |
| collection | DOAJ |
| description | Summary: Circovirus, comprising one capsid protein, is the smallest nonenveloped virus and induces lymphopenia. Circovirus can be used to explore the cell adhesion mechanism of nonenveloped viruses. We developed a single-molecule fluorescence resonance energy transfer (smFRET) assay to directly visualize the capsid's conformational feature. The capsid underwent reversible dynamic transformation between three conformations. The cell surface receptor heparan sulfate (HS) altered the dynamic equilibrium of the capsid to the high-FRET state, revealing the HS-binding region. Neutralizing antibodies restricted capsid transition to a low-FRET state, masking the HS-binding domain. The lack of positively charged amino acids in the HS-binding site reduced cell surface affinity and attenuated virus infectivity via conformational changes. These intrinsic characteristics of the capsid suggested that conformational dynamics is critical for the structural changes occurring upon cell surface receptor binding, supporting a dynamics-based mechanism of receptor binding. |
| first_indexed | 2024-12-19T15:10:21Z |
| format | Article |
| id | doaj.art-36b019abfe31402ab8646cd4ecd733e8 |
| institution | Directory Open Access Journal |
| issn | 2589-0042 |
| language | English |
| last_indexed | 2024-12-19T15:10:21Z |
| publishDate | 2020-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj.art-36b019abfe31402ab8646cd4ecd733e82022-12-21T20:16:19ZengElsevieriScience2589-00422020-10-012310101547Conformational Dynamics of Nonenveloped Circovirus Capsid to the Host Cell ReceptorJiarong Li0Jinyan Gu1Cui Lin2Jianwei Zhou3Shengnan Wang4Jin Lei5Fengcai Wen6Bo Sun7Jiyong Zhou8MOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, ChinaMOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, China; Corresponding authorMOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, ChinaMOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, ChinaMOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, ChinaInstitute of Immunology and College of Veterinary Medicine, Nanjing Agricultural University, Nanjing 210095, ChinaSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, ChinaSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, ChinaMOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, China; Collaborative Innovation Center and State Key Laboratory for Diagnosis and Treatment of Infectious Diseases, The First Affiliated Hospital, Zhejiang University, Hangzhou, Zhejiang 310058, China; Corresponding authorSummary: Circovirus, comprising one capsid protein, is the smallest nonenveloped virus and induces lymphopenia. Circovirus can be used to explore the cell adhesion mechanism of nonenveloped viruses. We developed a single-molecule fluorescence resonance energy transfer (smFRET) assay to directly visualize the capsid's conformational feature. The capsid underwent reversible dynamic transformation between three conformations. The cell surface receptor heparan sulfate (HS) altered the dynamic equilibrium of the capsid to the high-FRET state, revealing the HS-binding region. Neutralizing antibodies restricted capsid transition to a low-FRET state, masking the HS-binding domain. The lack of positively charged amino acids in the HS-binding site reduced cell surface affinity and attenuated virus infectivity via conformational changes. These intrinsic characteristics of the capsid suggested that conformational dynamics is critical for the structural changes occurring upon cell surface receptor binding, supporting a dynamics-based mechanism of receptor binding.http://www.sciencedirect.com/science/article/pii/S2589004220307392Molecular BiologyVirology |
| spellingShingle | Jiarong Li Jinyan Gu Cui Lin Jianwei Zhou Shengnan Wang Jin Lei Fengcai Wen Bo Sun Jiyong Zhou Conformational Dynamics of Nonenveloped Circovirus Capsid to the Host Cell Receptor iScience Molecular Biology Virology |
| title | Conformational Dynamics of Nonenveloped Circovirus Capsid to the Host Cell Receptor |
| title_full | Conformational Dynamics of Nonenveloped Circovirus Capsid to the Host Cell Receptor |
| title_fullStr | Conformational Dynamics of Nonenveloped Circovirus Capsid to the Host Cell Receptor |
| title_full_unstemmed | Conformational Dynamics of Nonenveloped Circovirus Capsid to the Host Cell Receptor |
| title_short | Conformational Dynamics of Nonenveloped Circovirus Capsid to the Host Cell Receptor |
| title_sort | conformational dynamics of nonenveloped circovirus capsid to the host cell receptor |
| topic | Molecular Biology Virology |
| url | http://www.sciencedirect.com/science/article/pii/S2589004220307392 |
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