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Registro Completo |
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Biblioteca(s): |
Embrapa Mandioca e Fruticultura. |
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Data corrente: |
05/11/2020 |
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Data da última atualização: |
05/11/2020 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
LEASTRO, M. O.; ASTUA, J. de F.; KITAJIMA, E. W.; PALLÁS, V.; SÁNCHEZ-NAVARRO, J. Á. |
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Afiliação: |
MIKHAIL OLIVEIRA LEASTRO, Instituto Biológico; JULIANA DE FREITAS ASTUA, CNPMF; ELLIOT WATANABE KITAJIMA, ESALQ; VICENTE PALLÁS, Universidad Politécnica de Valencia; JESÚS ÁNGEL SÁNCHEZ-NAVARRO, Universidad Politécnica de Valencia. |
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Título: |
Dichorhaviruses Movement Protein and Nucleoprotein Form a Protein Complex That May Be Required for Virus Spread and Interacts in vivo With Viral Movement-Related Cilevirus Proteins. |
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Ano de publicação: |
2020 |
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Fonte/Imprenta: |
Frontiers in Microbiology, v.11, November 2020. |
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Idioma: |
Inglês |
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Conteúdo: |
Brevipalpus-transmitted viruses (BTVs) belong to the genera Dichorhavirus and Cilevirus and are the main causal agents of the citrus leprosis (CL) disease. In this report, we explored aspects related to the movement mechanism mediated by dichorhaviruses movement proteins (MPs) and the homologous and heterologous interactions among viral proteins related to the movement of citrus leprosis-associated viruses. The membrane-spanning property and topology analysis of the nucleocapsid (N) and MP proteins from two dichorhaviruses revealed that the MPs are proteins tightly associated with the cell membrane, exposing their N- and C-termini to the cytoplasm and the inner part of the nucleus, whereas the N proteins are not membrane-associated. Subcellular localization analysis revealed the presence of dichorhavirus MPs at the cell surface and in the nucleus, while the phosphoproteins (P) were located exclusively in the nucleus and the N proteins in both the cytoplasm and the nucleus. Co-expression analysis with the MP, P, and N proteins showed an interaction network formed between them. We highlight the MP capability to partially redistribute the previously reported N-P core complex, redirecting a portion of the N from the nucleus to the plasmodesmata at the cell periphery, which indicates not only that the MP might guide the intracellular trafficking of the viral infective complex but also that the N protein may be associated with the cell-to-cell movement mechanism of dichorhaviruses. The movement functionality of these MPs was analyzed by using three movement-defective infectious systems. Also, the MP capacity to generate tubular structures on the protoplast surface by ectopic expression was analyzed. Finally, we evaluated the in vivo protein?protein interaction networks between the dichorhavirus MP and/or N proteins with the heterologous cilevirus movement components, which suggest a broad spectrum of interactions, highlighting those among capsid proteins (CP), MPs, and Ns from citrus leprosis-associated viruses. These data may aid in understanding the mixed infection process naturally observed in the field caused by distinct BTVs. Introduction MenosBrevipalpus-transmitted viruses (BTVs) belong to the genera Dichorhavirus and Cilevirus and are the main causal agents of the citrus leprosis (CL) disease. In this report, we explored aspects related to the movement mechanism mediated by dichorhaviruses movement proteins (MPs) and the homologous and heterologous interactions among viral proteins related to the movement of citrus leprosis-associated viruses. The membrane-spanning property and topology analysis of the nucleocapsid (N) and MP proteins from two dichorhaviruses revealed that the MPs are proteins tightly associated with the cell membrane, exposing their N- and C-termini to the cytoplasm and the inner part of the nucleus, whereas the N proteins are not membrane-associated. Subcellular localization analysis revealed the presence of dichorhavirus MPs at the cell surface and in the nucleus, while the phosphoproteins (P) were located exclusively in the nucleus and the N proteins in both the cytoplasm and the nucleus. Co-expression analysis with the MP, P, and N proteins showed an interaction network formed between them. We highlight the MP capability to partially redistribute the previously reported N-P core complex, redirecting a portion of the N from the nucleus to the plasmodesmata at the cell periphery, which indicates not only that the MP might guide the intracellular trafficking of the viral infective complex but also that the N protein may be associated with the cell-to-cell movement mechanism of dichorhaviruses... Mostrar Tudo |
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Thesagro: |
Vírus. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/217521/1/2020-Leastro-fmicb-11-571807-Dichorha.pdf
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Marc: |
LEADER 02807naa a2200181 a 4500
001 2126324
005 2020-11-05
008 2020 bl uuuu u00u1 u #d
100 1 $aLEASTRO, M. O.
245 $aDichorhaviruses Movement Protein and Nucleoprotein Form a Protein Complex That May Be Required for Virus Spread and Interacts in vivo With Viral Movement-Related Cilevirus Proteins.$h[electronic resource]
260 $c2020
520 $aBrevipalpus-transmitted viruses (BTVs) belong to the genera Dichorhavirus and Cilevirus and are the main causal agents of the citrus leprosis (CL) disease. In this report, we explored aspects related to the movement mechanism mediated by dichorhaviruses movement proteins (MPs) and the homologous and heterologous interactions among viral proteins related to the movement of citrus leprosis-associated viruses. The membrane-spanning property and topology analysis of the nucleocapsid (N) and MP proteins from two dichorhaviruses revealed that the MPs are proteins tightly associated with the cell membrane, exposing their N- and C-termini to the cytoplasm and the inner part of the nucleus, whereas the N proteins are not membrane-associated. Subcellular localization analysis revealed the presence of dichorhavirus MPs at the cell surface and in the nucleus, while the phosphoproteins (P) were located exclusively in the nucleus and the N proteins in both the cytoplasm and the nucleus. Co-expression analysis with the MP, P, and N proteins showed an interaction network formed between them. We highlight the MP capability to partially redistribute the previously reported N-P core complex, redirecting a portion of the N from the nucleus to the plasmodesmata at the cell periphery, which indicates not only that the MP might guide the intracellular trafficking of the viral infective complex but also that the N protein may be associated with the cell-to-cell movement mechanism of dichorhaviruses. The movement functionality of these MPs was analyzed by using three movement-defective infectious systems. Also, the MP capacity to generate tubular structures on the protoplast surface by ectopic expression was analyzed. Finally, we evaluated the in vivo protein?protein interaction networks between the dichorhavirus MP and/or N proteins with the heterologous cilevirus movement components, which suggest a broad spectrum of interactions, highlighting those among capsid proteins (CP), MPs, and Ns from citrus leprosis-associated viruses. These data may aid in understanding the mixed infection process naturally observed in the field caused by distinct BTVs. Introduction
650 $aVírus
700 1 $aASTUA, J. de F.
700 1 $aKITAJIMA, E. W.
700 1 $aPALLÁS, V.
700 1 $aSÁNCHEZ-NAVARRO, J. Á.
773 $tFrontiers in Microbiology$gv.11, November 2020.
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Registro original: |
Embrapa Mandioca e Fruticultura (CNPMF) |
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Biblioteca |
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Origem |
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Cutter |
Registro |
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Registro Completo
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Biblioteca(s): |
Embrapa Gado de Corte; Embrapa Gado de Leite. |
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Data corrente: |
30/12/2019 |
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Data da última atualização: |
30/12/2019 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
B - 1 |
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Autoria: |
BACANELLI, G.; OLARTE, L. C.; SILVA, M. R.; RODRIGUES, R. A.; CARNEIRO, P. A. M.; KANEENE, J. B.; PASQUATTI, T. N.; TAKATANI, H.; ZUMÁRRAGA, M. J.; ETGES, R. N.; ARAUJO, F. R.; VERBISCK, N. V. |
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Afiliação: |
GISELE BACANELLI, Universidade Federal de Mato Grosso do Sul - UFMS/Programa de Pós-Graduação em Biotecnologia e Biodiversidade da Região Centro-Oeste; LARISSA C. OLARTE, Universidade Federal de Mato Grosso do Sul - UFMS/Programa de Pós-Graduação Multicêntrica em Bioquímica e Biologia Molecular; MARCIO ROBERTO SILVA, CNPGL; RUDIELLE A. RODRIGUES, Universidade Federal de Mato Grosso do Sul - UFMS/Faculdade de Medicina Veterinária/Programa de Pós-Graduação em Ciências Veterinárias; PAULO A. M. CARNEIRO, Michigan State University/Center for Comparative Epidemiology; JOHN B. KANEENE, Michigan State University/Center for Comparative Epidemiology; TAYNARA N. PASQUATTI, Universidade Católica Dom Bosco - UCDB; HARUO TAKATANI, Agência de Defesa Agrícola do Amazonas; MARTIN J. ZUMÁRRAGA, Institute of Biotechnology, CICVyA/INTA; RODRIGO N. ETGES, Secretário de Agricultura, Pecuária e Irrigação de Porto Alegre; FLABIO RIBEIRO DE ARAUJO, CNPGC; NEWTON VALERIO VERBISCK, CNPGC. |
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Título: |
Matrix Assisted Laser Desorption Ionization-Time-of-Flight mass spectrometry identification of Mycobacterium bovis in Bovinae. |
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Ano de publicação: |
2019 |
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Fonte/Imprenta: |
Journal the Veterinary Medical Science, v. 81, n. 10, p.1400?1408, 2019. |
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Idioma: |
Inglês |
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Conteúdo: |
In this study, Matrix Assisted Laser Desorption Ionization-Time-of-Flight (MALDITOF) mass spectrometry was used to identify Mycobacterium bovis from cattle and buffalo tissue isolates from the North and South regions of Brazil, grown in solid medium and previously identified by Polymerase Chain Reaction (PCR) based on Region of Difference 4 (RD4), sequencing and spoligotyping. For this purpose, the protein extraction protocol and the mass spectra reference database were optimized for the identification of 80 clinical isolates of mycobacteria. As a result of this optimization, it was possible to identify and differentiate M. bovis from other members of the Mycobacterium tuberculosis complex with 100% specificity, 90.91% sensitivity and 91.25% reliability. MALDI-TOF MS methodology described herein provides successful identification of M. bovis within bovine/bubaline clinical samples, demonstrating its usefulness for bovine tuberculosis diagnosis in the future. |
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Palavras-Chave: |
Matrix Assisted Laser Desorption Ionization-Time-of-Flight (MALDI-TOF) mass spectrometry. |
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Thesaurus NAL: |
Bovine tuberculosis; Mycobacterium bovis BCG; Mycobacterium tuberculosis complex. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/207929/1/Matrix-Assisted-Laser-Desorption-Ionization.pdf
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Marc: |
LEADER 01994naa a2200301 a 4500
001 2117863
005 2019-12-30
008 2019 bl uuuu u00u1 u #d
100 1 $aBACANELLI, G.
245 $aMatrix Assisted Laser Desorption Ionization-Time-of-Flight mass spectrometry identification of Mycobacterium bovis in Bovinae.$h[electronic resource]
260 $c2019
520 $aIn this study, Matrix Assisted Laser Desorption Ionization-Time-of-Flight (MALDITOF) mass spectrometry was used to identify Mycobacterium bovis from cattle and buffalo tissue isolates from the North and South regions of Brazil, grown in solid medium and previously identified by Polymerase Chain Reaction (PCR) based on Region of Difference 4 (RD4), sequencing and spoligotyping. For this purpose, the protein extraction protocol and the mass spectra reference database were optimized for the identification of 80 clinical isolates of mycobacteria. As a result of this optimization, it was possible to identify and differentiate M. bovis from other members of the Mycobacterium tuberculosis complex with 100% specificity, 90.91% sensitivity and 91.25% reliability. MALDI-TOF MS methodology described herein provides successful identification of M. bovis within bovine/bubaline clinical samples, demonstrating its usefulness for bovine tuberculosis diagnosis in the future.
650 $aBovine tuberculosis
650 $aMycobacterium bovis BCG
650 $aMycobacterium tuberculosis complex
653 $aMatrix Assisted Laser Desorption Ionization-Time-of-Flight (MALDI-TOF) mass spectrometry
700 1 $aOLARTE, L. C.
700 1 $aSILVA, M. R.
700 1 $aRODRIGUES, R. A.
700 1 $aCARNEIRO, P. A. M.
700 1 $aKANEENE, J. B.
700 1 $aPASQUATTI, T. N.
700 1 $aTAKATANI, H.
700 1 $aZUMÁRRAGA, M. J.
700 1 $aETGES, R. N.
700 1 $aARAUJO, F. R.
700 1 $aVERBISCK, N. V.
773 $tJournal the Veterinary Medical Science$gv. 81, n. 10, p.1400?1408, 2019.
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Registro original: |
Embrapa Gado de Corte (CNPGC) |
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