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Distinct groups of RNA viruses associated with thermoacidophilic bacteria

Recent massive metatranscriptome mining substantially expanded the diversity of the bacterial RNA virome, suggesting that additional groups of riboviruses infecting bacterial hosts remain to be discovered. We employed full length double-stranded (ds) RNA sequencing for identification of riboviruses...

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Autores principales: Urayama, Syun-ichi, Fukudome, Akihito, Hirai, Miho, Okumura, Tomoyo, Nishimura, Yosuke, Takaki, Yoshihiro, Kurosawa, Norio, Koonin, Eugene V., Krupovic, Mart, Nunoura, Takuro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10542131/
https://www.ncbi.nlm.nih.gov/pubmed/37790367
http://dx.doi.org/10.1101/2023.07.02.547447
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author Urayama, Syun-ichi
Fukudome, Akihito
Hirai, Miho
Okumura, Tomoyo
Nishimura, Yosuke
Takaki, Yoshihiro
Kurosawa, Norio
Koonin, Eugene V.
Krupovic, Mart
Nunoura, Takuro
author_facet Urayama, Syun-ichi
Fukudome, Akihito
Hirai, Miho
Okumura, Tomoyo
Nishimura, Yosuke
Takaki, Yoshihiro
Kurosawa, Norio
Koonin, Eugene V.
Krupovic, Mart
Nunoura, Takuro
author_sort Urayama, Syun-ichi
collection PubMed
description Recent massive metatranscriptome mining substantially expanded the diversity of the bacterial RNA virome, suggesting that additional groups of riboviruses infecting bacterial hosts remain to be discovered. We employed full length double-stranded (ds) RNA sequencing for identification of riboviruses associated with microbial consortia dominated by bacteria and archaea in acidic hot springs in Japan. Whole sequences of two groups of multisegmented riboviruses genomes were obtained. One group, which we denoted hot spring riboviruses (HsRV), consists of unusual viruses with distinct RNA-dependent RNA polymerases (RdRPs) that seem to be intermediates between typical ribovirus RdRPs and viral reverse transcriptases. We also identified viruses encoding HsRV-like RdRPs in moderate aquatic environments, including marine water, river sediments and salt marsh, indicating that this previously overlooked ribovirus group is not restricted to the extreme ecosystem. The HsRV-like viruses are candidates for a distinct phylum or even kingdom within the viral realm Riboviria. The second group, denoted hot spring partiti-like viruses (HsPV), is a distinct branch within the family Partitiviridae. All genome segments in both these groups of viruses display the organization typical of bacterial riboviruses, where multiple open reading frames encoding individual proteins are preceded by ribosome-binding sites. Together with the identification in bacteria-dominated habitats, this genome architecture indicates that riboviruses of these distinct groups infect thermoacidophilic bacterial hosts.
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spelling pubmed-105421312023-10-03 Distinct groups of RNA viruses associated with thermoacidophilic bacteria Urayama, Syun-ichi Fukudome, Akihito Hirai, Miho Okumura, Tomoyo Nishimura, Yosuke Takaki, Yoshihiro Kurosawa, Norio Koonin, Eugene V. Krupovic, Mart Nunoura, Takuro bioRxiv Article Recent massive metatranscriptome mining substantially expanded the diversity of the bacterial RNA virome, suggesting that additional groups of riboviruses infecting bacterial hosts remain to be discovered. We employed full length double-stranded (ds) RNA sequencing for identification of riboviruses associated with microbial consortia dominated by bacteria and archaea in acidic hot springs in Japan. Whole sequences of two groups of multisegmented riboviruses genomes were obtained. One group, which we denoted hot spring riboviruses (HsRV), consists of unusual viruses with distinct RNA-dependent RNA polymerases (RdRPs) that seem to be intermediates between typical ribovirus RdRPs and viral reverse transcriptases. We also identified viruses encoding HsRV-like RdRPs in moderate aquatic environments, including marine water, river sediments and salt marsh, indicating that this previously overlooked ribovirus group is not restricted to the extreme ecosystem. The HsRV-like viruses are candidates for a distinct phylum or even kingdom within the viral realm Riboviria. The second group, denoted hot spring partiti-like viruses (HsPV), is a distinct branch within the family Partitiviridae. All genome segments in both these groups of viruses display the organization typical of bacterial riboviruses, where multiple open reading frames encoding individual proteins are preceded by ribosome-binding sites. Together with the identification in bacteria-dominated habitats, this genome architecture indicates that riboviruses of these distinct groups infect thermoacidophilic bacterial hosts. Cold Spring Harbor Laboratory 2023-07-03 /pmc/articles/PMC10542131/ /pubmed/37790367 http://dx.doi.org/10.1101/2023.07.02.547447 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator.
spellingShingle Article
Urayama, Syun-ichi
Fukudome, Akihito
Hirai, Miho
Okumura, Tomoyo
Nishimura, Yosuke
Takaki, Yoshihiro
Kurosawa, Norio
Koonin, Eugene V.
Krupovic, Mart
Nunoura, Takuro
Distinct groups of RNA viruses associated with thermoacidophilic bacteria
title Distinct groups of RNA viruses associated with thermoacidophilic bacteria
title_full Distinct groups of RNA viruses associated with thermoacidophilic bacteria
title_fullStr Distinct groups of RNA viruses associated with thermoacidophilic bacteria
title_full_unstemmed Distinct groups of RNA viruses associated with thermoacidophilic bacteria
title_short Distinct groups of RNA viruses associated with thermoacidophilic bacteria
title_sort distinct groups of rna viruses associated with thermoacidophilic bacteria
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10542131/
https://www.ncbi.nlm.nih.gov/pubmed/37790367
http://dx.doi.org/10.1101/2023.07.02.547447
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