Structural Insights into the Human Astrovirus Capsid
Astroviruses (AstVs) are non-enveloped, positive single-stranded RNA viruses that cause a wide range of inflammatory diseases in mammalian and avian hosts. The T = 3 viral capsid is unique in its ability to infect host cells in a process driven by host proteases. Intercellular protease cleavages all...
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Format: | Article |
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MDPI AG
2021-05-01
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Online Access: | https://www.mdpi.com/1999-4915/13/5/821 |
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author | Matthew Ykema Yizhi J. Tao |
author_facet | Matthew Ykema Yizhi J. Tao |
author_sort | Matthew Ykema |
collection | DOAJ |
description | Astroviruses (AstVs) are non-enveloped, positive single-stranded RNA viruses that cause a wide range of inflammatory diseases in mammalian and avian hosts. The T = 3 viral capsid is unique in its ability to infect host cells in a process driven by host proteases. Intercellular protease cleavages allow for viral egress from a cell, while extracellular cleavages allow for the virus to enter a new host cell to initiate infection. High-resolution models of the capsid core indicate a large, exposed region enriched with protease cleavage sites. The virus spike protein allows for binding to target cells and is the major target for naturally occurring and engineered neutralizing antibodies. During maturation, the capsid goes through significant structural changes including the loss of many surface spikes. The capsid interacts with host membranes during the virus life cycle at multiple stages such as assembly, host cell entry and exit. This review will cover recent findings and insights related to the structure of the capsid and its function. Further understanding of the viral capsid structure and maturation process can contribute to new vaccines, gastric therapeutics, and viral engineering applications. |
first_indexed | 2024-03-10T11:45:50Z |
format | Article |
id | doaj.art-fb87be71955141a3833d1d1b1e001c07 |
institution | Directory Open Access Journal |
issn | 1999-4915 |
language | English |
last_indexed | 2024-03-10T11:45:50Z |
publishDate | 2021-05-01 |
publisher | MDPI AG |
record_format | Article |
series | Viruses |
spelling | doaj.art-fb87be71955141a3833d1d1b1e001c072023-11-21T18:10:05ZengMDPI AGViruses1999-49152021-05-0113582110.3390/v13050821Structural Insights into the Human Astrovirus CapsidMatthew Ykema0Yizhi J. Tao1Department of BioSciences, Rice University, Houston, TX 77005, USADepartment of BioSciences, Rice University, Houston, TX 77005, USAAstroviruses (AstVs) are non-enveloped, positive single-stranded RNA viruses that cause a wide range of inflammatory diseases in mammalian and avian hosts. The T = 3 viral capsid is unique in its ability to infect host cells in a process driven by host proteases. Intercellular protease cleavages allow for viral egress from a cell, while extracellular cleavages allow for the virus to enter a new host cell to initiate infection. High-resolution models of the capsid core indicate a large, exposed region enriched with protease cleavage sites. The virus spike protein allows for binding to target cells and is the major target for naturally occurring and engineered neutralizing antibodies. During maturation, the capsid goes through significant structural changes including the loss of many surface spikes. The capsid interacts with host membranes during the virus life cycle at multiple stages such as assembly, host cell entry and exit. This review will cover recent findings and insights related to the structure of the capsid and its function. Further understanding of the viral capsid structure and maturation process can contribute to new vaccines, gastric therapeutics, and viral engineering applications.https://www.mdpi.com/1999-4915/13/5/821astroviruscapsidstructurecrystallographyvirus maturation |
spellingShingle | Matthew Ykema Yizhi J. Tao Structural Insights into the Human Astrovirus Capsid Viruses astrovirus capsid structure crystallography virus maturation |
title | Structural Insights into the Human Astrovirus Capsid |
title_full | Structural Insights into the Human Astrovirus Capsid |
title_fullStr | Structural Insights into the Human Astrovirus Capsid |
title_full_unstemmed | Structural Insights into the Human Astrovirus Capsid |
title_short | Structural Insights into the Human Astrovirus Capsid |
title_sort | structural insights into the human astrovirus capsid |
topic | astrovirus capsid structure crystallography virus maturation |
url | https://www.mdpi.com/1999-4915/13/5/821 |
work_keys_str_mv | AT matthewykema structuralinsightsintothehumanastroviruscapsid AT yizhijtao structuralinsightsintothehumanastroviruscapsid |