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| Registros recuperados : 550 | |
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Registro Completo |
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Biblioteca(s): |
Biblioteca Rui Tendinha. |
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Data corrente: |
23/02/2023 |
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Data da última atualização: |
25/04/2023 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
MAURASTONI, M.; ANTUNES, T. F. S.; ABREU, E. F. M.; RIBEIRO, S. G.; MEHTA, A.; SANCHES, M. M.; FONTES, W.; KITAJIMA, E. W.; CRUZ, F. T.; SANTOS, A. M. C.; VENTURA, J. A.; GOMES, A. C. M. M.; ZERBINI, F. M.; SOSA-ACOSTA, P.; NOGUEIRA, F. C. S.; RODRIGUES, S. P.; ARAGÃO, F. J. L.; WHITFIELD, A. E.; FERNANDES, P. M. B. |
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Afiliação: |
Marlonni Maurastoni, UFES; Tathiana F. Sá Antunes, UFES; Emanuel F. M. Abreu, Embrapa Recursos Genéticos e Biotecnologia; Simone G. Ribeiro, Embrapa Recursos Genéticos e Biotecnologia; Angela Mehta, Embrapa Recursos Genéticos e Biotecnologia; Marcio M. Sanches, Embrapa Recursos Genéticos e Biotecnologia; Wagner Fontes, UNB; Elliot W. Kitajima, USP; Fabiano T. Cruz, UFES; Alexandre M. C. Santos, UFES; Jose Aires Ventura, Incaper; Ana C. M. M. Gomes, Embrapa Recursos Genéticos e Biotecnologia; F. Murilo Zerbini, UFV; Patricia Sosa-Acosta, UFRJ; Fábio C. S. Nogueira, UFRJ; Silas P. Rodrigues, UFRJ; Francisco J. L. Aragão, Embrapa Recursos Genéticos e Biotecnologia; Anna E. Whitfield, North Carolina State University; Patricia M. B. Fernandes, UFES. |
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Título: |
A capsid protein fragment of a Toti-like Virus Found in Carica papaya Latex interacts with the 50S ribosomal protein L17 |
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Ano de publicação: |
2023 |
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Fonte/Imprenta: |
Viruses, v. 15, n. 541, p. 1-20, 2023. |
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DOI: |
10.3390/v15020541 |
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Idioma: |
Inglês |
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Conteúdo: |
Papaya sticky disease is caused by the association of a fusagra-like and an umbra-like virus, named papaya meleira virus (PMeV) and papaya meleira virus 2 (PMeV2), respectively. Both viral genomes are encapsidated in particles formed by the PMeV ORF1 product, which has the potential to encode a protein with 1563 amino acids (aa). However, the structural components of the viral capsid are unknown. To characterize the structural proteins of PMeV and PMeV2, virions were purified from Carica papaya latex. SDS-PAGE analysis of purified virus revealed two major proteins of ~40 kDa and ~55 kDa. Amino-terminal sequencing of the ~55 kDa protein and LC-MS/MS of purified virions indicated that this protein starts at aa 263 of the deduced ORF1 product as a result of either degradation or proteolytic processing. A yeast two-hybrid assay was used to identify Arabidopsis proteins interacting with two PMeV ORF1 product fragments (aa 321?670 and 961?1200). The 50S ribosomal protein L17 (AtRPL17) was identified as potentially associated with modulated translation-related proteins. In plant cells, AtRPL17 co-localized and interacted with the PMeV ORF1 fragments. These findings support the hypothesis that the interaction between PMeV/PMeV2 structural proteins and RPL17 is important for virus?host interactions. |
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Palavras-Chave: |
Meleira. |
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Thesagro: |
Carica Papaya; Mamão; Proteína; Vírus. |
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Categoria do assunto: |
-- |
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URL: |
https://biblioteca.incaper.es.gov.br/digital/bitstream/item/4389/1/A-Capsid-Protein-Fragment-of-a-Toti-like-Virus-2023.pdf
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Marc: |
LEADER 02456naa a2200409 a 4500
001 1024693
005 2023-04-25
008 2023 bl uuuu u00u1 u #d
024 7 $a10.3390/v15020541$2DOI
100 1 $aMAURASTONI, M.
245 $aA capsid protein fragment of a Toti-like Virus Found in Carica papaya Latex interacts with the 50S ribosomal protein L17$h[electronic resource]
260 $c2023
520 $aPapaya sticky disease is caused by the association of a fusagra-like and an umbra-like virus, named papaya meleira virus (PMeV) and papaya meleira virus 2 (PMeV2), respectively. Both viral genomes are encapsidated in particles formed by the PMeV ORF1 product, which has the potential to encode a protein with 1563 amino acids (aa). However, the structural components of the viral capsid are unknown. To characterize the structural proteins of PMeV and PMeV2, virions were purified from Carica papaya latex. SDS-PAGE analysis of purified virus revealed two major proteins of ~40 kDa and ~55 kDa. Amino-terminal sequencing of the ~55 kDa protein and LC-MS/MS of purified virions indicated that this protein starts at aa 263 of the deduced ORF1 product as a result of either degradation or proteolytic processing. A yeast two-hybrid assay was used to identify Arabidopsis proteins interacting with two PMeV ORF1 product fragments (aa 321?670 and 961?1200). The 50S ribosomal protein L17 (AtRPL17) was identified as potentially associated with modulated translation-related proteins. In plant cells, AtRPL17 co-localized and interacted with the PMeV ORF1 fragments. These findings support the hypothesis that the interaction between PMeV/PMeV2 structural proteins and RPL17 is important for virus?host interactions.
650 $aCarica Papaya
650 $aMamão
650 $aProteína
650 $aVírus
653 $aMeleira
700 1 $aANTUNES, T. F. S.
700 1 $aABREU, E. F. M.
700 1 $aRIBEIRO, S. G.
700 1 $aMEHTA, A.
700 1 $aSANCHES, M. M.
700 1 $aFONTES, W.
700 1 $aKITAJIMA, E. W.
700 1 $aCRUZ, F. T.
700 1 $aSANTOS, A. M. C.
700 1 $aVENTURA, J. A.
700 1 $aGOMES, A. C. M. M.
700 1 $aZERBINI, F. M.
700 1 $aSOSA-ACOSTA, P.
700 1 $aNOGUEIRA, F. C. S.
700 1 $aRODRIGUES, S. P.
700 1 $aARAGÃO, F. J. L.
700 1 $aWHITFIELD, A. E.
700 1 $aFERNANDES, P. M. B.
773 $tViruses$gv. 15, n. 541, p. 1-20, 2023.
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Biblioteca Rui Tendinha (BRT) |
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