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Proteome expansion in the Potyviridae evolutionary radiation
Potyviridae, the largest family of known RNA viruses (realm Riboviria), belongs to the picorna-like supergroup and has important agricultural and ecological impacts. Potyvirid genomes are translated into polyproteins, which are in turn hydrolyzed to release mature products. Recent sequencing efforts...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9249622/ https://www.ncbi.nlm.nih.gov/pubmed/35195244 http://dx.doi.org/10.1093/femsre/fuac011 |
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author | Pasin, Fabio Daròs, José-Antonio Tzanetakis, Ioannis E |
author_facet | Pasin, Fabio Daròs, José-Antonio Tzanetakis, Ioannis E |
author_sort | Pasin, Fabio |
collection | PubMed |
description | Potyviridae, the largest family of known RNA viruses (realm Riboviria), belongs to the picorna-like supergroup and has important agricultural and ecological impacts. Potyvirid genomes are translated into polyproteins, which are in turn hydrolyzed to release mature products. Recent sequencing efforts revealed an unprecedented number of potyvirids with a rich variability in gene content and genomic layouts. Here, we review the heterogeneity of non-core modules that expand the structural and functional diversity of the potyvirid proteomes. We provide a family-wide classification of P1 proteinases into the functional Types A and B, and discuss pretty interesting sweet potato potyviral ORF (PISPO), putative zinc fingers, and alkylation B (AlkB)—non-core modules found within P1 cistrons. The atypical inosine triphosphate pyrophosphatase (ITPase/HAM1), as well as the pseudo tobacco mosaic virus-like coat protein (TMV-like CP) are discussed alongside homologs of unrelated virus taxa. Family-wide abundance of the multitasking helper component proteinase (HC-pro) is revised. Functional connections between non-core modules are highlighted to support host niche adaptation and immune evasion as main drivers of the Potyviridae evolutionary radiation. Potential biotechnological and synthetic biology applications of potyvirid leader proteinases and non-core modules are finally explored. |
format | Online Article Text |
id | pubmed-9249622 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-92496222022-07-05 Proteome expansion in the Potyviridae evolutionary radiation Pasin, Fabio Daròs, José-Antonio Tzanetakis, Ioannis E FEMS Microbiol Rev Review Article Potyviridae, the largest family of known RNA viruses (realm Riboviria), belongs to the picorna-like supergroup and has important agricultural and ecological impacts. Potyvirid genomes are translated into polyproteins, which are in turn hydrolyzed to release mature products. Recent sequencing efforts revealed an unprecedented number of potyvirids with a rich variability in gene content and genomic layouts. Here, we review the heterogeneity of non-core modules that expand the structural and functional diversity of the potyvirid proteomes. We provide a family-wide classification of P1 proteinases into the functional Types A and B, and discuss pretty interesting sweet potato potyviral ORF (PISPO), putative zinc fingers, and alkylation B (AlkB)—non-core modules found within P1 cistrons. The atypical inosine triphosphate pyrophosphatase (ITPase/HAM1), as well as the pseudo tobacco mosaic virus-like coat protein (TMV-like CP) are discussed alongside homologs of unrelated virus taxa. Family-wide abundance of the multitasking helper component proteinase (HC-pro) is revised. Functional connections between non-core modules are highlighted to support host niche adaptation and immune evasion as main drivers of the Potyviridae evolutionary radiation. Potential biotechnological and synthetic biology applications of potyvirid leader proteinases and non-core modules are finally explored. Oxford University Press 2022-02-23 /pmc/articles/PMC9249622/ /pubmed/35195244 http://dx.doi.org/10.1093/femsre/fuac011 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of FEMS. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Pasin, Fabio Daròs, José-Antonio Tzanetakis, Ioannis E Proteome expansion in the Potyviridae evolutionary radiation |
title | Proteome expansion in the Potyviridae evolutionary radiation |
title_full | Proteome expansion in the Potyviridae evolutionary radiation |
title_fullStr | Proteome expansion in the Potyviridae evolutionary radiation |
title_full_unstemmed | Proteome expansion in the Potyviridae evolutionary radiation |
title_short | Proteome expansion in the Potyviridae evolutionary radiation |
title_sort | proteome expansion in the potyviridae evolutionary radiation |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9249622/ https://www.ncbi.nlm.nih.gov/pubmed/35195244 http://dx.doi.org/10.1093/femsre/fuac011 |
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