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Atomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy
Bufavirus strain 1 (BuV1), a member of the Protoparvovirus genus of the Parvoviridae, was first isolated from fecal samples of children with acute diarrhea in Burkina Faso. Since this initial discovery, BuVs have been isolated in several countries, including Finland, the Netherlands, and Bhutan, in...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5795435/ https://www.ncbi.nlm.nih.gov/pubmed/29300333 http://dx.doi.org/10.3390/v10010022 |
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author | Ilyas, Maria Mietzsch, Mario Kailasan, Shweta Väisänen, Elina Luo, Mengxiao Chipman, Paul Smith, J. Kennon Kurian, Justin Sousa, Duncan McKenna, Robert Söderlund-Venermo, Maria Agbandje-McKenna, Mavis |
author_facet | Ilyas, Maria Mietzsch, Mario Kailasan, Shweta Väisänen, Elina Luo, Mengxiao Chipman, Paul Smith, J. Kennon Kurian, Justin Sousa, Duncan McKenna, Robert Söderlund-Venermo, Maria Agbandje-McKenna, Mavis |
author_sort | Ilyas, Maria |
collection | PubMed |
description | Bufavirus strain 1 (BuV1), a member of the Protoparvovirus genus of the Parvoviridae, was first isolated from fecal samples of children with acute diarrhea in Burkina Faso. Since this initial discovery, BuVs have been isolated in several countries, including Finland, the Netherlands, and Bhutan, in pediatric patients exhibiting similar symptoms. Towards their characterization, the structures of virus-like particles of BuV1, BuV2, and BuV3, the current known genotypes, have been determined by cryo-electron microscopy and image reconstruction to 2.84, 3.79, and 3.25 Å, respectively. The BuVs, 65–73% identical in amino acid sequence, conserve the major viral protein, VP2, structure and general capsid surface features of parvoviruses. These include a core β-barrel (βB-βI), α-helix A, and large surface loops inserted between these elements in VP2. The capsid contains depressions at the icosahedral 2-fold and around the 5-fold axes, and has three separated protrusions surrounding the 3-fold axes. Structure comparison among the BuVs and to available parvovirus structures revealed capsid surface variations and capsid 3-fold protrusions that depart from the single pinwheel arrangement of the animal protoparvoviruses. These structures provide a platform to begin the molecular characterization of these potentially pathogenic viruses. |
format | Online Article Text |
id | pubmed-5795435 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-57954352018-02-09 Atomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy Ilyas, Maria Mietzsch, Mario Kailasan, Shweta Väisänen, Elina Luo, Mengxiao Chipman, Paul Smith, J. Kennon Kurian, Justin Sousa, Duncan McKenna, Robert Söderlund-Venermo, Maria Agbandje-McKenna, Mavis Viruses Article Bufavirus strain 1 (BuV1), a member of the Protoparvovirus genus of the Parvoviridae, was first isolated from fecal samples of children with acute diarrhea in Burkina Faso. Since this initial discovery, BuVs have been isolated in several countries, including Finland, the Netherlands, and Bhutan, in pediatric patients exhibiting similar symptoms. Towards their characterization, the structures of virus-like particles of BuV1, BuV2, and BuV3, the current known genotypes, have been determined by cryo-electron microscopy and image reconstruction to 2.84, 3.79, and 3.25 Å, respectively. The BuVs, 65–73% identical in amino acid sequence, conserve the major viral protein, VP2, structure and general capsid surface features of parvoviruses. These include a core β-barrel (βB-βI), α-helix A, and large surface loops inserted between these elements in VP2. The capsid contains depressions at the icosahedral 2-fold and around the 5-fold axes, and has three separated protrusions surrounding the 3-fold axes. Structure comparison among the BuVs and to available parvovirus structures revealed capsid surface variations and capsid 3-fold protrusions that depart from the single pinwheel arrangement of the animal protoparvoviruses. These structures provide a platform to begin the molecular characterization of these potentially pathogenic viruses. MDPI 2018-01-04 /pmc/articles/PMC5795435/ /pubmed/29300333 http://dx.doi.org/10.3390/v10010022 Text en © 2018 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Ilyas, Maria Mietzsch, Mario Kailasan, Shweta Väisänen, Elina Luo, Mengxiao Chipman, Paul Smith, J. Kennon Kurian, Justin Sousa, Duncan McKenna, Robert Söderlund-Venermo, Maria Agbandje-McKenna, Mavis Atomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy |
title | Atomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy |
title_full | Atomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy |
title_fullStr | Atomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy |
title_full_unstemmed | Atomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy |
title_short | Atomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy |
title_sort | atomic resolution structures of human bufaviruses determined by cryo-electron microscopy |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5795435/ https://www.ncbi.nlm.nih.gov/pubmed/29300333 http://dx.doi.org/10.3390/v10010022 |
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