Poorly conserved p15 proteins of cileviruses retain elements of common ancestry and putative functionality: a theoretical assessment on the evolution of cilevirus genomes.

Detalhes bibliográficos
Autor(a) principal: RAMOS-GONZÁLEZ, P. L.
Data de Publicação: 2021
Outros Autores: PONS, T., CHABI-JESUS, C., ARENA, G. D., ASTUA, J. de F.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
Texto Completo: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1136833
https://doi.org/10.3389/fpls.2021.771983
Resumo: The genus Cilevirus groups enveloped single-stranded (+) RNA virus members of the family Kitaviridae, order Martellivirales. Proteins P15, scarcely conserved polypeptides encoded by cileviruses, have no apparent homologs in public databases. Accordingly, the open reading frames (ORFs) p15, located at the 5?-end of the viral RNA2 molecules, are considered orphan genes (ORFans). In this study, we have delved into ORFs p15 and the relatively poorly understood biochemical properties of the proteins P15 to posit their importance for viruses across the genus and theorize on their origin. We detected that the ORFs p15 are under purifying selection and that, in some viral strains, the use of synonymous codons is biased, which might be a sign of adaptation to their plant hosts. Despite the high amino acid sequence divergence, proteins P15 show the conserved motif [FY]-L-x(3)-[FL]-H-x-x-[LIV]-S-C-x-C-x(2)-C-x-G-x-C, which occurs exclusively in members of this protein family. Proteins P15 also show a common predicted 3D structure that resembles the helical scaffold of the protein ORF49 encoded by radinoviruses and the phosphoprotein C-terminal domain of mononegavirids. Based on the 3D structural similarities of P15, we suggest elements of common ancestry, conserved functionality, and relevant amino acid residues. We conclude by postulating a plausible evolutionary trajectory of ORFans p15 and the 5?-end of the RNA2 of cileviruses considering both protein fold superpositions and comparative genomic analyses with the closest kitaviruses, negeviruses, nege/kita-like viruses, and unrelated viruses that share the ecological niches of cileviruses.
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spelling Poorly conserved p15 proteins of cileviruses retain elements of common ancestry and putative functionality: a theoretical assessment on the evolution of cilevirus genomes.ProteínaVírusGenomaThe genus Cilevirus groups enveloped single-stranded (+) RNA virus members of the family Kitaviridae, order Martellivirales. Proteins P15, scarcely conserved polypeptides encoded by cileviruses, have no apparent homologs in public databases. Accordingly, the open reading frames (ORFs) p15, located at the 5?-end of the viral RNA2 molecules, are considered orphan genes (ORFans). In this study, we have delved into ORFs p15 and the relatively poorly understood biochemical properties of the proteins P15 to posit their importance for viruses across the genus and theorize on their origin. We detected that the ORFs p15 are under purifying selection and that, in some viral strains, the use of synonymous codons is biased, which might be a sign of adaptation to their plant hosts. Despite the high amino acid sequence divergence, proteins P15 show the conserved motif [FY]-L-x(3)-[FL]-H-x-x-[LIV]-S-C-x-C-x(2)-C-x-G-x-C, which occurs exclusively in members of this protein family. Proteins P15 also show a common predicted 3D structure that resembles the helical scaffold of the protein ORF49 encoded by radinoviruses and the phosphoprotein C-terminal domain of mononegavirids. Based on the 3D structural similarities of P15, we suggest elements of common ancestry, conserved functionality, and relevant amino acid residues. We conclude by postulating a plausible evolutionary trajectory of ORFans p15 and the 5?-end of the RNA2 of cileviruses considering both protein fold superpositions and comparative genomic analyses with the closest kitaviruses, negeviruses, nege/kita-like viruses, and unrelated viruses that share the ecological niches of cileviruses.PEDRO L. RAMOS-GONZÁLEZ, Instituto Biológico de São Paulo; TIRSO PONS, CNB-CSIC; CAMILA CHABI-JESUS, Instituto Biológico de São Paulo; GABRIELLA DIAS ARENA, Instituto Biológico de São Paulo; JULIANA DE FREITAS ASTUA, CNPMF.RAMOS-GONZÁLEZ, P. L.PONS, T.CHABI-JESUS, C.ARENA, G. D.ASTUA, J. de F.2021-11-30T15:00:24Z2021-11-30T15:00:24Z2021-11-302021info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleFrontiers in Plant Science, November, 2021.1664-462Xhttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1136833https://doi.org/10.3389/fpls.2021.771983enginfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)instacron:EMBRAPA2021-11-30T15:00:35Zoai:www.alice.cnptia.embrapa.br:doc/1136833Repositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestopendoar:21542021-11-30T15:00:35falseRepositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestcg-riaa@embrapa.bropendoar:21542021-11-30T15:00:35Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)false
dc.title.none.fl_str_mv Poorly conserved p15 proteins of cileviruses retain elements of common ancestry and putative functionality: a theoretical assessment on the evolution of cilevirus genomes.
title Poorly conserved p15 proteins of cileviruses retain elements of common ancestry and putative functionality: a theoretical assessment on the evolution of cilevirus genomes.
spellingShingle Poorly conserved p15 proteins of cileviruses retain elements of common ancestry and putative functionality: a theoretical assessment on the evolution of cilevirus genomes.
RAMOS-GONZÁLEZ, P. L.
Proteína
Vírus
Genoma
title_short Poorly conserved p15 proteins of cileviruses retain elements of common ancestry and putative functionality: a theoretical assessment on the evolution of cilevirus genomes.
title_full Poorly conserved p15 proteins of cileviruses retain elements of common ancestry and putative functionality: a theoretical assessment on the evolution of cilevirus genomes.
title_fullStr Poorly conserved p15 proteins of cileviruses retain elements of common ancestry and putative functionality: a theoretical assessment on the evolution of cilevirus genomes.
title_full_unstemmed Poorly conserved p15 proteins of cileviruses retain elements of common ancestry and putative functionality: a theoretical assessment on the evolution of cilevirus genomes.
title_sort Poorly conserved p15 proteins of cileviruses retain elements of common ancestry and putative functionality: a theoretical assessment on the evolution of cilevirus genomes.
author RAMOS-GONZÁLEZ, P. L.
author_facet RAMOS-GONZÁLEZ, P. L.
PONS, T.
CHABI-JESUS, C.
ARENA, G. D.
ASTUA, J. de F.
author_role author
author2 PONS, T.
CHABI-JESUS, C.
ARENA, G. D.
ASTUA, J. de F.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv PEDRO L. RAMOS-GONZÁLEZ, Instituto Biológico de São Paulo; TIRSO PONS, CNB-CSIC; CAMILA CHABI-JESUS, Instituto Biológico de São Paulo; GABRIELLA DIAS ARENA, Instituto Biológico de São Paulo; JULIANA DE FREITAS ASTUA, CNPMF.
dc.contributor.author.fl_str_mv RAMOS-GONZÁLEZ, P. L.
PONS, T.
CHABI-JESUS, C.
ARENA, G. D.
ASTUA, J. de F.
dc.subject.por.fl_str_mv Proteína
Vírus
Genoma
topic Proteína
Vírus
Genoma
description The genus Cilevirus groups enveloped single-stranded (+) RNA virus members of the family Kitaviridae, order Martellivirales. Proteins P15, scarcely conserved polypeptides encoded by cileviruses, have no apparent homologs in public databases. Accordingly, the open reading frames (ORFs) p15, located at the 5?-end of the viral RNA2 molecules, are considered orphan genes (ORFans). In this study, we have delved into ORFs p15 and the relatively poorly understood biochemical properties of the proteins P15 to posit their importance for viruses across the genus and theorize on their origin. We detected that the ORFs p15 are under purifying selection and that, in some viral strains, the use of synonymous codons is biased, which might be a sign of adaptation to their plant hosts. Despite the high amino acid sequence divergence, proteins P15 show the conserved motif [FY]-L-x(3)-[FL]-H-x-x-[LIV]-S-C-x-C-x(2)-C-x-G-x-C, which occurs exclusively in members of this protein family. Proteins P15 also show a common predicted 3D structure that resembles the helical scaffold of the protein ORF49 encoded by radinoviruses and the phosphoprotein C-terminal domain of mononegavirids. Based on the 3D structural similarities of P15, we suggest elements of common ancestry, conserved functionality, and relevant amino acid residues. We conclude by postulating a plausible evolutionary trajectory of ORFans p15 and the 5?-end of the RNA2 of cileviruses considering both protein fold superpositions and comparative genomic analyses with the closest kitaviruses, negeviruses, nege/kita-like viruses, and unrelated viruses that share the ecological niches of cileviruses.
publishDate 2021
dc.date.none.fl_str_mv 2021-11-30T15:00:24Z
2021-11-30T15:00:24Z
2021-11-30
2021
dc.type.driver.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv Frontiers in Plant Science, November, 2021.
1664-462X
http://www.alice.cnptia.embrapa.br/alice/handle/doc/1136833
https://doi.org/10.3389/fpls.2021.771983
identifier_str_mv Frontiers in Plant Science, November, 2021.
1664-462X
url http://www.alice.cnptia.embrapa.br/alice/handle/doc/1136833
https://doi.org/10.3389/fpls.2021.771983
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv reponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
instacron:EMBRAPA
instname_str Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
instacron_str EMBRAPA
institution EMBRAPA
reponame_str Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
collection Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
repository.name.fl_str_mv Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
repository.mail.fl_str_mv cg-riaa@embrapa.br
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