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Cryo-EM structure of ssDNA bacteriophage ΦCjT23 provides insight into early virus evolution

The origin of viruses remains an open question. While lack of detectable sequence similarity hampers the analysis of distantly related viruses, structural biology investigations of conserved capsid protein structures facilitate the study of distant evolutionary relationships. Here we characterize th...

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Autores principales: Kejzar, Nejc, Laanto, Elina, Rissanen, Ilona, Abrishami, Vahid, Selvaraj, Muniyandi, Moineau, Sylvain, Ravantti, Janne, Sundberg, Lotta-Riina, Huiskonen, Juha T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9719478/
https://www.ncbi.nlm.nih.gov/pubmed/36463224
http://dx.doi.org/10.1038/s41467-022-35123-6
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author Kejzar, Nejc
Laanto, Elina
Rissanen, Ilona
Abrishami, Vahid
Selvaraj, Muniyandi
Moineau, Sylvain
Ravantti, Janne
Sundberg, Lotta-Riina
Huiskonen, Juha T.
author_facet Kejzar, Nejc
Laanto, Elina
Rissanen, Ilona
Abrishami, Vahid
Selvaraj, Muniyandi
Moineau, Sylvain
Ravantti, Janne
Sundberg, Lotta-Riina
Huiskonen, Juha T.
author_sort Kejzar, Nejc
collection PubMed
description The origin of viruses remains an open question. While lack of detectable sequence similarity hampers the analysis of distantly related viruses, structural biology investigations of conserved capsid protein structures facilitate the study of distant evolutionary relationships. Here we characterize the lipid-containing ssDNA temperate bacteriophage ΦCjT23, which infects Flavobacterium sp. (Bacteroidetes). We report ΦCjT23-like sequences in the genome of strains belonging to several Flavobacterium species. The virion structure determined by cryogenic electron microscopy reveals similarities to members of the viral kingdom Bamfordvirae that currently consists solely of dsDNA viruses with a major capsid protein composed of two upright β-sandwiches. The minimalistic structure of ΦCjT23 suggests that this phage serves as a model for the last common ancestor between ssDNA and dsDNA viruses in the Bamfordvirae. Both ΦCjT23 and the related phage FLiP infect Flavobacterium species found in several environments, suggesting that these types of viruses have a global distribution and a shared evolutionary origin. Detailed comparisons to related, more complex viruses not only expand our knowledge about this group of viruses but also provide a rare glimpse into early virus evolution.
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spelling pubmed-97194782022-12-05 Cryo-EM structure of ssDNA bacteriophage ΦCjT23 provides insight into early virus evolution Kejzar, Nejc Laanto, Elina Rissanen, Ilona Abrishami, Vahid Selvaraj, Muniyandi Moineau, Sylvain Ravantti, Janne Sundberg, Lotta-Riina Huiskonen, Juha T. Nat Commun Article The origin of viruses remains an open question. While lack of detectable sequence similarity hampers the analysis of distantly related viruses, structural biology investigations of conserved capsid protein structures facilitate the study of distant evolutionary relationships. Here we characterize the lipid-containing ssDNA temperate bacteriophage ΦCjT23, which infects Flavobacterium sp. (Bacteroidetes). We report ΦCjT23-like sequences in the genome of strains belonging to several Flavobacterium species. The virion structure determined by cryogenic electron microscopy reveals similarities to members of the viral kingdom Bamfordvirae that currently consists solely of dsDNA viruses with a major capsid protein composed of two upright β-sandwiches. The minimalistic structure of ΦCjT23 suggests that this phage serves as a model for the last common ancestor between ssDNA and dsDNA viruses in the Bamfordvirae. Both ΦCjT23 and the related phage FLiP infect Flavobacterium species found in several environments, suggesting that these types of viruses have a global distribution and a shared evolutionary origin. Detailed comparisons to related, more complex viruses not only expand our knowledge about this group of viruses but also provide a rare glimpse into early virus evolution. Nature Publishing Group UK 2022-12-03 /pmc/articles/PMC9719478/ /pubmed/36463224 http://dx.doi.org/10.1038/s41467-022-35123-6 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Kejzar, Nejc
Laanto, Elina
Rissanen, Ilona
Abrishami, Vahid
Selvaraj, Muniyandi
Moineau, Sylvain
Ravantti, Janne
Sundberg, Lotta-Riina
Huiskonen, Juha T.
Cryo-EM structure of ssDNA bacteriophage ΦCjT23 provides insight into early virus evolution
title Cryo-EM structure of ssDNA bacteriophage ΦCjT23 provides insight into early virus evolution
title_full Cryo-EM structure of ssDNA bacteriophage ΦCjT23 provides insight into early virus evolution
title_fullStr Cryo-EM structure of ssDNA bacteriophage ΦCjT23 provides insight into early virus evolution
title_full_unstemmed Cryo-EM structure of ssDNA bacteriophage ΦCjT23 provides insight into early virus evolution
title_short Cryo-EM structure of ssDNA bacteriophage ΦCjT23 provides insight into early virus evolution
title_sort cryo-em structure of ssdna bacteriophage φcjt23 provides insight into early virus evolution
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9719478/
https://www.ncbi.nlm.nih.gov/pubmed/36463224
http://dx.doi.org/10.1038/s41467-022-35123-6
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