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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...

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Autores principales: Wang, Ivy, Gupta, Sandeep K., Ems, Guillaume, Jayawardena, Nadishka, Strauss, Mike, Bostina, Mihnea
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
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.
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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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