Structural Requirements and Plasticity of Receptor-Binding Domain in Human Coronavirus Spike
The most recent human coronaviruses including severe acute respiratory syndrome coronavirus-2 causing severe respiratory tract infection and high pathogenicity bring significant global public health concerns. Infections are initiated by recognizing host cell receptors by coronavirus spike protein S1...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-07-01
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| Series: | Frontiers in Molecular Biosciences |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmolb.2022.930931/full |
| _version_ | 1818529712693051392 |
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| author | Yajuan Li Peiyi Zheng Tingting Liu Cuixiao Shi Bo Wang Yuanhong Xu Tengchuan Jin |
| author_facet | Yajuan Li Peiyi Zheng Tingting Liu Cuixiao Shi Bo Wang Yuanhong Xu Tengchuan Jin |
| author_sort | Yajuan Li |
| collection | DOAJ |
| description | The most recent human coronaviruses including severe acute respiratory syndrome coronavirus-2 causing severe respiratory tract infection and high pathogenicity bring significant global public health concerns. Infections are initiated by recognizing host cell receptors by coronavirus spike protein S1 subunit, and then S2 mediates membrane fusion. However, human coronavirus spikes undergo frequent mutation, which may result in diverse pathogenesis and infectivity. In this review, we summarize some of these recent structural and mutational characteristics of RBD of human coronavirus spike protein and their interaction with specific human cell receptors and analyze the structural requirements and plasticity of RBD. Stability of spike protein, affinity toward receptor, virus fitness, and infectivity are the factors controlling the viral tropisms. Thus, understanding the molecular details of RBDs and their mutations is critical in deciphering virus evolution. Structural information of spike and receptors of human coronaviruses not only reveals the molecular mechanism of host–microbe interaction and pathogenesis but also helps develop effective drug to control these infectious pathogens and cope with the future emerging coronavirus outbreaks. |
| first_indexed | 2024-12-11T17:10:22Z |
| format | Article |
| id | doaj.art-c503e2305a5340f58d835983a1261db4 |
| institution | Directory Open Access Journal |
| issn | 2296-889X |
| language | English |
| last_indexed | 2024-12-11T17:10:22Z |
| publishDate | 2022-07-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Biosciences |
| spelling | doaj.art-c503e2305a5340f58d835983a1261db42022-12-22T00:57:34ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2022-07-01910.3389/fmolb.2022.930931930931Structural Requirements and Plasticity of Receptor-Binding Domain in Human Coronavirus SpikeYajuan Li0Peiyi Zheng1Tingting Liu2Cuixiao Shi3Bo Wang4Yuanhong Xu5Tengchuan Jin6Department of Clinical Laboratory, The First Affiliated Hospital of Anhui Medical University, Hefei, ChinaLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Basic Medical Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, ChinaDepartment of Clinical Laboratory, The First Affiliated Hospital of Anhui Medical University, Hefei, ChinaDepartment of Clinical Laboratory, The First Affiliated Hospital of Anhui Medical University, Hefei, ChinaDepartment of Clinical Laboratory, The First Affiliated Hospital of Anhui Medical University, Hefei, ChinaDepartment of Clinical Laboratory, The First Affiliated Hospital of Anhui Medical University, Hefei, ChinaLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Basic Medical Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, ChinaThe most recent human coronaviruses including severe acute respiratory syndrome coronavirus-2 causing severe respiratory tract infection and high pathogenicity bring significant global public health concerns. Infections are initiated by recognizing host cell receptors by coronavirus spike protein S1 subunit, and then S2 mediates membrane fusion. However, human coronavirus spikes undergo frequent mutation, which may result in diverse pathogenesis and infectivity. In this review, we summarize some of these recent structural and mutational characteristics of RBD of human coronavirus spike protein and their interaction with specific human cell receptors and analyze the structural requirements and plasticity of RBD. Stability of spike protein, affinity toward receptor, virus fitness, and infectivity are the factors controlling the viral tropisms. Thus, understanding the molecular details of RBDs and their mutations is critical in deciphering virus evolution. Structural information of spike and receptors of human coronaviruses not only reveals the molecular mechanism of host–microbe interaction and pathogenesis but also helps develop effective drug to control these infectious pathogens and cope with the future emerging coronavirus outbreaks.https://www.frontiersin.org/articles/10.3389/fmolb.2022.930931/fullhuman coronavirusreceptor-binding domainstructureplasticitymutation |
| spellingShingle | Yajuan Li Peiyi Zheng Tingting Liu Cuixiao Shi Bo Wang Yuanhong Xu Tengchuan Jin Structural Requirements and Plasticity of Receptor-Binding Domain in Human Coronavirus Spike Frontiers in Molecular Biosciences human coronavirus receptor-binding domain structure plasticity mutation |
| title | Structural Requirements and Plasticity of Receptor-Binding Domain in Human Coronavirus Spike |
| title_full | Structural Requirements and Plasticity of Receptor-Binding Domain in Human Coronavirus Spike |
| title_fullStr | Structural Requirements and Plasticity of Receptor-Binding Domain in Human Coronavirus Spike |
| title_full_unstemmed | Structural Requirements and Plasticity of Receptor-Binding Domain in Human Coronavirus Spike |
| title_short | Structural Requirements and Plasticity of Receptor-Binding Domain in Human Coronavirus Spike |
| title_sort | structural requirements and plasticity of receptor binding domain in human coronavirus spike |
| topic | human coronavirus receptor-binding domain structure plasticity mutation |
| url | https://www.frontiersin.org/articles/10.3389/fmolb.2022.930931/full |
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