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Cryo-EM Structure of a Possum Enterovirus
Enteroviruses (EVs) represent a substantial concern to global health. Here, we present the cryo-EM structure of a non-human enterovirus, EV-F4, isolated from the Australian brushtail possum to assess the structural diversity of these picornaviruses. The capsid structure, determined to ~3 Å resolutio...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8879876/ https://www.ncbi.nlm.nih.gov/pubmed/35215909 http://dx.doi.org/10.3390/v14020318 |
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author | Wang, Ivy Gupta, Sandeep K. Ems, Guillaume Jayawardena, Nadishka Strauss, Mike Bostina, Mihnea |
author_facet | Wang, Ivy Gupta, Sandeep K. Ems, Guillaume Jayawardena, Nadishka Strauss, Mike Bostina, Mihnea |
author_sort | Wang, Ivy |
collection | PubMed |
description | Enteroviruses (EVs) represent a substantial concern to global health. Here, we present the cryo-EM structure of a non-human enterovirus, EV-F4, isolated from the Australian brushtail possum to assess the structural diversity of these picornaviruses. The capsid structure, determined to ~3 Å resolution by single particle analysis, exhibits a largely smooth surface, similar to EV-F3 (formerly BEV-2). Although the cellular receptor is not known, the absence of charged residues on the outer surface of the canyon suggest a different receptor type than for EV-F3. Density for the pocket factor is clear, with the entrance to the pocket being smaller than for other enteroviruses. |
format | Online Article Text |
id | pubmed-8879876 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88798762022-02-26 Cryo-EM Structure of a Possum Enterovirus Wang, Ivy Gupta, Sandeep K. Ems, Guillaume Jayawardena, Nadishka Strauss, Mike Bostina, Mihnea Viruses Article Enteroviruses (EVs) represent a substantial concern to global health. Here, we present the cryo-EM structure of a non-human enterovirus, EV-F4, isolated from the Australian brushtail possum to assess the structural diversity of these picornaviruses. The capsid structure, determined to ~3 Å resolution by single particle analysis, exhibits a largely smooth surface, similar to EV-F3 (formerly BEV-2). Although the cellular receptor is not known, the absence of charged residues on the outer surface of the canyon suggest a different receptor type than for EV-F3. Density for the pocket factor is clear, with the entrance to the pocket being smaller than for other enteroviruses. MDPI 2022-02-03 /pmc/articles/PMC8879876/ /pubmed/35215909 http://dx.doi.org/10.3390/v14020318 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Wang, Ivy Gupta, Sandeep K. Ems, Guillaume Jayawardena, Nadishka Strauss, Mike Bostina, Mihnea Cryo-EM Structure of a Possum Enterovirus |
title | Cryo-EM Structure of a Possum Enterovirus |
title_full | Cryo-EM Structure of a Possum Enterovirus |
title_fullStr | Cryo-EM Structure of a Possum Enterovirus |
title_full_unstemmed | Cryo-EM Structure of a Possum Enterovirus |
title_short | Cryo-EM Structure of a Possum Enterovirus |
title_sort | cryo-em structure of a possum enterovirus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8879876/ https://www.ncbi.nlm.nih.gov/pubmed/35215909 http://dx.doi.org/10.3390/v14020318 |
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