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| 1. |  | KUHN, J. H.; ABE, J.; ADKINS, S.; ALKHOVSKY, S. V.; AVSIC-ZUPANC, T.; AYLLÓN, M. A.; BAHL, J.; BALKEMA-BUSCHMANN, A.; BALLINGER, M. J.; BARANWAL, V. K.; BEER, M.; BEJERMAN, N.; BERGERON, É.; BIEDENKOPF, N.; BLAIR, C. D.; BLASDELL, K. R.; BLOUIN, A. G.; BRADFUTE, S. B.; BRIESE, T.; BROWN, P. A.; BUCHHOLZ, U. J.; BUCHMEIER, M. J.; BUKREYEV, A.; BURT, F.; BÜTTNER, C.; CALISHER, C. H.; CAO, M.; CASAS, I.; CHANDRAN, K.; CHARREL, R. N.; CHATURVEDI, K. K.; CHOOI, K. M.; CRANE, A.; BÓ, E. D.; TORRE, J. C. de L.; SOUZA, W. M. de; SWART, R. L. de; DEBAT, H.; DHEILLY, N. M.; PAOLA, N. D.; SERIO, F. D.; DIETZGEN, R. G.; DIGIARO, M.; DREXLER, J. F.; DUPREX, W. P.; DÜRRWALD, R.; EASTON, A. J.; ELBEAINO, T.; ERGÜNAY, K.; FENG, G.; FIRTH, A. E.; FOOKS, A. R.; FORMENTY, P. B. H.; FREITAS-ASTÚA, J.; GAGO-ZACHERT, S.; GARCÍA, M. L.; GARCÍA-SASTRE, A.; GARRISON, A. R.; GASKIN, T. R.; GONG, W.; GONZALEZ, J. J.; BELLOCQ, J. de; GRIFFITHS, A.; GROSCHUP, M. H.; GÜNTHER, I.; GÜNTHER, S.; HAMMOND, J.; HASEGAWA, Y.; HAYASHI, K.; HEPOJOKI, J.; HIGGINS, C. M.; HONGO, S.; HORIE, M.; HUGHES, H. R.; HUME, A. J.; HYNDMAN, T. H.; IKEDA, K.; JIANG, D.; JONSON, G. B.; JUNGLEN, S.; KLEMPA, B.; KLINGSTRÖM, J.; KONDO, H.; KOONIN, E. V.; KRUPOVIC, M.; KUBOTA, K.; KURATH, G.; LAENEN, L.; LAMBERT, A. J.; LI, J.; LI, J.; LIU, R.; LUKASHEVICH, I. S.; MACDIARMID, R. M.; MAES, P.; MARKLEWITZ, M.; MARSHALL, S. H.; MARZANO, S. L.; MCCAULEY, J. W.; MIRAZIMI, A.; MÜHLBERGER, E.; NABESHIMA, T.; NAIDU, R.; NATSUAKI, T.; NAVARRO, B.; JOSÉ; NERIYA, Y.; NETESOV, S. V.; NEUMANN, G.; NOWOTNY, N.; NUNES, M. R. T.; OCHOA-CORONA, F. M.; OKADA, T.; PALACIOS, G.; PALLÁS, V.; PAPA, A.; PARASKEVOPOULOU, S.; PARRISH, C. R.; PAUVOLID-CORRÊA, A.; PAWESKA, J. T.; PÉREZ, D. R.; PFAFF, F.; PLEMPER, R. K.; POSTLER, T. S.; RABBIDGE, L. O.; RADOSHITZKY, S. R.; RAMOS-GONZÁLEZ, P. L.; REHANEK, M.; RESENDE, R. O.; REYES, C. A.; RODRIGUES, T. C. S.; ROMANOWSKI, V.; RUBBENSTROTH, D.; RUBINO, L.; RUNSTADLER, J. A.; SABANADZOVIC, S.; SADIQ, S.; SALVATO, M. S.; SASAYA, T.; SCHWEMMLE, M.; SHARPE, S. R.; SHI, M.; SHIMOMOTO, Y.; SIDHARTHAN, V. K.; SIRONI, M.; SMITHER, S.; SONG, J.; SPANN, K. M.; SPENGLER, J. R.; STENGLEIN, M. D.; TAKADA, A.; TAKEYAMA, S.; TATARA, A.; TESH, R. B.; THORNBURG, N. J.; TIAN, X.; TISCHLER, N. D.; TOMITAKA, Y.; TOMONAGA, K.; TORDO, N.; TU, C.; TURINA, M.; TZANETAKIS, I. E.; VAIRA, A. M.; HOOGEN, B. V. D.; VANMECHELEN, B.; VASILAKIS, N.; VERBEEK, M.; BARGEN, S. V.; WADA, J.; WAHL, V.; WALKER, P. J.; WALTZEK, T. B.; WHITFIELD, A. E.; WOLF, Y. I.; XIA, H.; XYLOGIANNI, E.; YANAGISAWA, H.; YANO, K.; YE, G.; YUAN, Z.; ZERBINI, F. M.; ZHANG, G.; ZHANG, S.; ZHANG, Y.; ZHAO, L.; OKLAND, A. L. Annual (2023) taxonomic update of RNA-directed RNA polymerase-encoding negative-sense RNA viruses (realm Riboviria: kingdom Orthornavirae: phylum Negarnaviricota). Journal of General Virology, v. 104, n. 8, 2023., Microbiology Society, 2023.| Biblioteca(s): Embrapa Mandioca e Fruticultura. |
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Registro Completo
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Biblioteca(s): |
Embrapa Mandioca e Fruticultura. |
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Data corrente: |
04/02/2014 |
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Data da última atualização: |
19/05/2023 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 2 |
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Autoria: |
SILVA, F. A. C.; PIROVANI, C. P.; MENEZES, S.; PUNGARTNIK, C.; SANTIAGO, A. S.; COSTA, M. G. C.; MICHELI, F.; GESTEIRA, A. da S. |
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Afiliação: |
F. A. C. SILVA, UESC; C. P. PIROVANI, UESC; S. MENEZES, UESC; C. PUNGARTNIK, UESC; A. S. SANTIAGO, UESC; M. G. C. COSTA, UESC; F. MICHELI, Agricultural Research for Development; ABELMON DA SILVA GESTEIRA, CNPMF. |
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Título: |
Proteomic response of Moniliophthora perniciosa exposed to pathogenesis-related protein-10 from Theobroma cacao. |
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Ano de publicação: |
2013 |
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Fonte/Imprenta: |
Genetics and Molecular Research, v.12, n. 4, p. 4855-4868, 2013. |
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ISSN: |
1676-5680 |
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Idioma: |
Inglês |
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Conteúdo: |
TcPR-10, a member of the pathogenesis-related protein 10 family, was identified in EST library of interactions between Theobroma cacao and Moniliophthora perniciosa. TcPR-10 has been shown to have antifungal and ribonuclease activities in vitro. This study aimed to identify proteins that are differentially expressed in M. perniciosa in response to TcPR-10 through a proteomic analysis. The fungal hyphae were subjected to one of four treatments: control treatment or 30-, 60- or 120-min treatment with the TcPR-10 protein. Two-dimensional maps revealed 191 differentially expressed proteins, 55 of which were identified by mass spectrometry. The proteins identified in all treatments were divided into the following classes: cell metabolism, stress response, zinc binding, phosphorylation mechanism, transport, autophagy, DNA repair, and oxidoreductases. The predominant class was stress-response proteins (29%), such as heat shock proteins; these proteins exhibited the highest expression levels relative to the control treatment and are known to trigger defense mechanisms against cytotoxic drugs as well as TcPR-10. Oxidoreductases (25%) were overexpressed in the control and in 30-min treatments but exhibited reduced expression at 120 min. These proteins are involved in the repair of damage caused by oxidative stress due to the contact with TcPR- 10. Consistent with the antifungal activity of TcPR-10, several proteins identified were related to detoxification, autophagy or were involved in mechanisms for maintaining fungal homeostasis, such as ergosterol biosynthesis. These results show that the sensitivity of the fungus to TcPR-10 involves several biochemical routes, clarifying the possible modes of action of this antifungal protein. MenosTcPR-10, a member of the pathogenesis-related protein 10 family, was identified in EST library of interactions between Theobroma cacao and Moniliophthora perniciosa. TcPR-10 has been shown to have antifungal and ribonuclease activities in vitro. This study aimed to identify proteins that are differentially expressed in M. perniciosa in response to TcPR-10 through a proteomic analysis. The fungal hyphae were subjected to one of four treatments: control treatment or 30-, 60- or 120-min treatment with the TcPR-10 protein. Two-dimensional maps revealed 191 differentially expressed proteins, 55 of which were identified by mass spectrometry. The proteins identified in all treatments were divided into the following classes: cell metabolism, stress response, zinc binding, phosphorylation mechanism, transport, autophagy, DNA repair, and oxidoreductases. The predominant class was stress-response proteins (29%), such as heat shock proteins; these proteins exhibited the highest expression levels relative to the control treatment and are known to trigger defense mechanisms against cytotoxic drugs as well as TcPR-10. Oxidoreductases (25%) were overexpressed in the control and in 30-min treatments but exhibited reduced expression at 120 min. These proteins are involved in the repair of damage caused by oxidative stress due to the contact with TcPR- 10. Consistent with the antifungal activity of TcPR-10, several proteins identified were related to detoxification, autophagy or were involved ... Mostrar Tudo |
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Palavras-Chave: |
Differentially expressed proteins; Stress-response proteins. |
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Thesagro: |
Cacau; Doença de planta; Theobroma Cacao. |
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Thesaurus NAL: |
Oxidoreductases; Pathogenesis-related proteins. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02677naa a2200301 a 4500
001 1978540
005 2023-05-19
008 2013 bl uuuu u00u1 u #d
022 $a1676-5680
100 1 $aSILVA, F. A. C.
245 $aProteomic response of Moniliophthora perniciosa exposed to pathogenesis-related protein-10 from Theobroma cacao.$h[electronic resource]
260 $c2013
520 $aTcPR-10, a member of the pathogenesis-related protein 10 family, was identified in EST library of interactions between Theobroma cacao and Moniliophthora perniciosa. TcPR-10 has been shown to have antifungal and ribonuclease activities in vitro. This study aimed to identify proteins that are differentially expressed in M. perniciosa in response to TcPR-10 through a proteomic analysis. The fungal hyphae were subjected to one of four treatments: control treatment or 30-, 60- or 120-min treatment with the TcPR-10 protein. Two-dimensional maps revealed 191 differentially expressed proteins, 55 of which were identified by mass spectrometry. The proteins identified in all treatments were divided into the following classes: cell metabolism, stress response, zinc binding, phosphorylation mechanism, transport, autophagy, DNA repair, and oxidoreductases. The predominant class was stress-response proteins (29%), such as heat shock proteins; these proteins exhibited the highest expression levels relative to the control treatment and are known to trigger defense mechanisms against cytotoxic drugs as well as TcPR-10. Oxidoreductases (25%) were overexpressed in the control and in 30-min treatments but exhibited reduced expression at 120 min. These proteins are involved in the repair of damage caused by oxidative stress due to the contact with TcPR- 10. Consistent with the antifungal activity of TcPR-10, several proteins identified were related to detoxification, autophagy or were involved in mechanisms for maintaining fungal homeostasis, such as ergosterol biosynthesis. These results show that the sensitivity of the fungus to TcPR-10 involves several biochemical routes, clarifying the possible modes of action of this antifungal protein.
650 $aOxidoreductases
650 $aPathogenesis-related proteins
650 $aCacau
650 $aDoença de planta
650 $aTheobroma Cacao
653 $aDifferentially expressed proteins
653 $aStress-response proteins
700 1 $aPIROVANI, C. P.
700 1 $aMENEZES, S.
700 1 $aPUNGARTNIK, C.
700 1 $aSANTIAGO, A. S.
700 1 $aCOSTA, M. G. C.
700 1 $aMICHELI, F.
700 1 $aGESTEIRA, A. da S.
773 $tGenetics and Molecular Research$gv.12, n. 4, p. 4855-4868, 2013.
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