Structural study of enteroviruses
<p>Enteroviruses comprise a genus of picornaviruses causing global morbidity and regional outbreaks. These viruses are the causative agents of severe, widespread diseases such as hand-foot-and-mouth disease, poliomyelitis and aseptic meningitis. Although they have been studied for decades, few...
Main Author: | |
---|---|
Other Authors: | |
Format: | Thesis |
Language: | English |
Published: |
2023
|
_version_ | 1797112116649394176 |
---|---|
author | Qin, L |
author2 | Stuart, D |
author_facet | Stuart, D Qin, L |
author_sort | Qin, L |
collection | OXFORD |
description | <p>Enteroviruses comprise a genus of picornaviruses causing global morbidity and regional outbreaks. These viruses are the causative agents of severe, widespread diseases such as hand-foot-and-mouth disease, poliomyelitis and aseptic meningitis. Although they have been studied for decades, few vaccines or drugs are in use. Indeed, many structural details of enterovirus infection, immune response and life cycle remain unknown. Solving these structural mysteries may provide crucial information that aids the elimination of these infectious particles.</p>
<p>The work described in this thesis extends our structural understanding of enteroviruses detailing the receptor binding manner of Echovirus 11 and closely related enteroviruses (chapter 3) and the polyclonal antibody response to poliovirus (chapter 4). To support these studies, a ‘SyRe’ protocol is described for analysis of enterovirus capsid proteins at protomer-scale, and pentamer-scale for the efficient detection of polyclonal antibody attachment (chapter 4). Finally, an <em>in-vitro</em> host cell membrane mimetic system is optimized to visualize virus-cell attachment and membrane penetration (chapter 5), together with powerful EM tools this will facilitate obtaining detailed structural information of virus entry in the near future.</p> |
first_indexed | 2024-03-07T08:19:41Z |
format | Thesis |
id | oxford-uuid:18b673f7-1dd3-47b4-a8f4-1f73c5eb1e33 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T08:19:41Z |
publishDate | 2023 |
record_format | dspace |
spelling | oxford-uuid:18b673f7-1dd3-47b4-a8f4-1f73c5eb1e332024-01-26T09:18:04ZStructural study of enterovirusesThesishttp://purl.org/coar/resource_type/c_db06uuid:18b673f7-1dd3-47b4-a8f4-1f73c5eb1e33EnglishHyrax Deposit2023Qin, LStuart, DFry, E<p>Enteroviruses comprise a genus of picornaviruses causing global morbidity and regional outbreaks. These viruses are the causative agents of severe, widespread diseases such as hand-foot-and-mouth disease, poliomyelitis and aseptic meningitis. Although they have been studied for decades, few vaccines or drugs are in use. Indeed, many structural details of enterovirus infection, immune response and life cycle remain unknown. Solving these structural mysteries may provide crucial information that aids the elimination of these infectious particles.</p> <p>The work described in this thesis extends our structural understanding of enteroviruses detailing the receptor binding manner of Echovirus 11 and closely related enteroviruses (chapter 3) and the polyclonal antibody response to poliovirus (chapter 4). To support these studies, a ‘SyRe’ protocol is described for analysis of enterovirus capsid proteins at protomer-scale, and pentamer-scale for the efficient detection of polyclonal antibody attachment (chapter 4). Finally, an <em>in-vitro</em> host cell membrane mimetic system is optimized to visualize virus-cell attachment and membrane penetration (chapter 5), together with powerful EM tools this will facilitate obtaining detailed structural information of virus entry in the near future.</p> |
spellingShingle | Qin, L Structural study of enteroviruses |
title | Structural study of enteroviruses |
title_full | Structural study of enteroviruses |
title_fullStr | Structural study of enteroviruses |
title_full_unstemmed | Structural study of enteroviruses |
title_short | Structural study of enteroviruses |
title_sort | structural study of enteroviruses |
work_keys_str_mv | AT qinl structuralstudyofenteroviruses |