Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike Variants
The global pandemic of COVID-19 caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has significantly affected every human life and overloaded the health care system worldwide. Limited therapeutic options combined with the consecutive waves of the infection and emergence of novel...
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MDPI AG
2022-06-01
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Series: | Viruses |
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Online Access: | https://www.mdpi.com/1999-4915/14/6/1255 |
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author | Dibya Ghimire Yang Han Maolin Lu |
author_facet | Dibya Ghimire Yang Han Maolin Lu |
author_sort | Dibya Ghimire |
collection | DOAJ |
description | The global pandemic of COVID-19 caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has significantly affected every human life and overloaded the health care system worldwide. Limited therapeutic options combined with the consecutive waves of the infection and emergence of novel SARS-CoV-2 variants, especially variants of concern (VOCs), have prolonged the COVID-19 pandemic and challenged its control. The Spike (S) protein on the surface of SARS-CoV-2 is the primary target exposed to the host and essential for virus entry into cells. The parental (Wuhan-Hu-1 or USA/WA1 strain) S protein is the virus-specific component of currently implemented vaccines. However, S is most prone to mutations, potentially shifting the dynamics of virus-host interactions by affecting S conformational/structural profiles. Scientists have rapidly resolved atomic structures of S VOCs and elucidated molecular details of these mutations, which can inform the design of S-directed novel therapeutics and broadly protective vaccines. Here, we discuss recent findings on S-associated virus transmissibility and immune evasion of SARS-CoV-2 VOCs and experimental approaches used to profile these properties. We summarize the structural studies that document the structural flexibility/plasticity of S VOCs and the potential roles of accumulated mutations on S structures and functions. We focus on the molecular interpretation of structures of the S variants and its insights into the molecular mechanism underlying antibody evasion and host cell-receptor binding. |
first_indexed | 2024-03-09T22:14:31Z |
format | Article |
id | doaj.art-a479169eb45b4ebda2fc1e07f002d377 |
institution | Directory Open Access Journal |
issn | 1999-4915 |
language | English |
last_indexed | 2024-03-09T22:14:31Z |
publishDate | 2022-06-01 |
publisher | MDPI AG |
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series | Viruses |
spelling | doaj.art-a479169eb45b4ebda2fc1e07f002d3772023-11-23T19:26:19ZengMDPI AGViruses1999-49152022-06-01146125510.3390/v14061255Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike VariantsDibya Ghimire0Yang Han1Maolin Lu2Department of Cellular and Molecular Biology, University of Texas Health Science Center, Tyler, TX 75708, USADepartment of Cellular and Molecular Biology, University of Texas Health Science Center, Tyler, TX 75708, USADepartment of Cellular and Molecular Biology, University of Texas Health Science Center, Tyler, TX 75708, USAThe global pandemic of COVID-19 caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has significantly affected every human life and overloaded the health care system worldwide. Limited therapeutic options combined with the consecutive waves of the infection and emergence of novel SARS-CoV-2 variants, especially variants of concern (VOCs), have prolonged the COVID-19 pandemic and challenged its control. The Spike (S) protein on the surface of SARS-CoV-2 is the primary target exposed to the host and essential for virus entry into cells. The parental (Wuhan-Hu-1 or USA/WA1 strain) S protein is the virus-specific component of currently implemented vaccines. However, S is most prone to mutations, potentially shifting the dynamics of virus-host interactions by affecting S conformational/structural profiles. Scientists have rapidly resolved atomic structures of S VOCs and elucidated molecular details of these mutations, which can inform the design of S-directed novel therapeutics and broadly protective vaccines. Here, we discuss recent findings on S-associated virus transmissibility and immune evasion of SARS-CoV-2 VOCs and experimental approaches used to profile these properties. We summarize the structural studies that document the structural flexibility/plasticity of S VOCs and the potential roles of accumulated mutations on S structures and functions. We focus on the molecular interpretation of structures of the S variants and its insights into the molecular mechanism underlying antibody evasion and host cell-receptor binding.https://www.mdpi.com/1999-4915/14/6/1255SARS-CoV-2variants of concernSpike proteinsstructuresconformationsimmune evasion |
spellingShingle | Dibya Ghimire Yang Han Maolin Lu Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike Variants Viruses SARS-CoV-2 variants of concern Spike proteins structures conformations immune evasion |
title | Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike Variants |
title_full | Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike Variants |
title_fullStr | Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike Variants |
title_full_unstemmed | Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike Variants |
title_short | Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike Variants |
title_sort | structural plasticity and immune evasion of sars cov 2 spike variants |
topic | SARS-CoV-2 variants of concern Spike proteins structures conformations immune evasion |
url | https://www.mdpi.com/1999-4915/14/6/1255 |
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