A conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensis
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | https://repositorio.unifesp.br/handle/11600/57446 http://dx.doi.org/10.1093/femsyr/fow047 |
Resumo: | Paracoccidioides brasiliensis and P. lutzii, thermally dimorphic fungi, are the causative agents of paracoccidioidomycosis (PCM). Paracoccidioides infection occurs when conidia or mycelium fragments are inhaled by the host, which causes the Paracoccidioides cells to transition to the yeast form. The development of disease requires conidia inside the host alveoli to differentiate into yeast cells in a temperature-dependent manner. We describe the presence of a two-component signal transduction system in P. brasiliensis, which we investigated by expression analysis of a hypothetical protein gene (PADG_07579) that showed high similarity with the dimorphism-regulating histidine kinase (DRK1) gene of Blastomyces dermatitidis and Histoplasma capsulatum. This gene was sensitive to environmental redox changes, which was demonstrated by a dose-dependent decrease in transcript levels after peroxide stimulation and a subtler decrease in transcript levels after NO stimulation. Furthermore, the higher PbDRK1 levels after treatment with increasing NaCl concentrations suggest that this histidine kinase can play a role as osmosensing. In the mycelium-yeast (M -> Y) transition, PbDRK1 mRNA expression increased 14-fold after 24 h incubation at 37A degrees C, consistent with similar observations in other virulent fungi. These results demonstrate that the PbDRK1 gene is differentially expressed during the dimorphic M -> Y transition. Finally, when P. brasiliensis mycelium cells were exposed to a histidine kinase inhibitor and incubated at 37A degrees C, there was a delay in the dimorphic M -> Y transition, suggesting that histidine kinases could be targets of interest for PCM therapy. |
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Chaves, Alison F. A. [UNIFESP]Navarro, Marina V. [UNIFESP]Castilho, Daniele G. [UNIFESP]Calado, Juliana C. P. [UNIFESP]Conceicao, Palloma M. [UNIFESP]Batista, Wagner L. [UNIFESP]2020-08-14T13:43:56Z2020-08-14T13:43:56Z2016Fems Yeast Research. Oxford, v. 16, n. 5, p. -, 2016.1567-1356https://repositorio.unifesp.br/handle/11600/57446http://dx.doi.org/10.1093/femsyr/fow047WOS000383231100005.pdf10.1093/femsyr/fow047WOS:000383231100005Paracoccidioides brasiliensis and P. lutzii, thermally dimorphic fungi, are the causative agents of paracoccidioidomycosis (PCM). Paracoccidioides infection occurs when conidia or mycelium fragments are inhaled by the host, which causes the Paracoccidioides cells to transition to the yeast form. The development of disease requires conidia inside the host alveoli to differentiate into yeast cells in a temperature-dependent manner. We describe the presence of a two-component signal transduction system in P. brasiliensis, which we investigated by expression analysis of a hypothetical protein gene (PADG_07579) that showed high similarity with the dimorphism-regulating histidine kinase (DRK1) gene of Blastomyces dermatitidis and Histoplasma capsulatum. This gene was sensitive to environmental redox changes, which was demonstrated by a dose-dependent decrease in transcript levels after peroxide stimulation and a subtler decrease in transcript levels after NO stimulation. Furthermore, the higher PbDRK1 levels after treatment with increasing NaCl concentrations suggest that this histidine kinase can play a role as osmosensing. In the mycelium-yeast (M -> Y) transition, PbDRK1 mRNA expression increased 14-fold after 24 h incubation at 37A degrees C, consistent with similar observations in other virulent fungi. These results demonstrate that the PbDRK1 gene is differentially expressed during the dimorphic M -> Y transition. Finally, when P. brasiliensis mycelium cells were exposed to a histidine kinase inhibitor and incubated at 37A degrees C, there was a delay in the dimorphic M -> Y transition, suggesting that histidine kinases could be targets of interest for PCM therapy.CNPq (Conselho Nacional de Desenvolvimento Cientifico e Tecnologico/Brazil)FAPESP (Fundacao de Amparo a Pesquisa do Estado de Sao Paulo/Brazil)Univ Fed Sao Paulo, Dept Microbiol Imunol & Parasitol, Unidade Jose Alencar, St Sao Nicolau 210,4 Floor, BR-04023900 Sao Paulo, BrazilUniv Fed Sao Paulo, Dept Ciencias Farmaceut, R Sao Nicolau 210, BR-09913030 Diadema, SP, BrazilUniv Fed Sao Paulo, Dept Microbiol Imunol & Parasitol, Unidade Jose Alencar, St Sao Nicolau 210,4 Floor, BR-04023900 Sao Paulo, BrazilUniv Fed Sao Paulo, Dept Ciencias Farmaceut, R Sao Nicolau 210, BR-09913030 Diadema, SP, BrazilCNPq: 478023/2013-8FAPESP: 2014/13961-1FAPESP: 2015/09727-6Web of Science-engOxford Univ PressFems Yeast Researchdimorphismhistidine kinasephosphorelayParacoccidioidesA conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensisinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleOxford165info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000383231100005.pdfapplication/pdf7005901${dspace.ui.url}/bitstream/11600/57446/1/WOS000383231100005.pdf4ed70ffc6f5eae1a353149ce958d2e19MD51open accessTEXTWOS000383231100005.pdf.txtWOS000383231100005.pdf.txtExtracted texttext/plain49661${dspace.ui.url}/bitstream/11600/57446/8/WOS000383231100005.pdf.txtcaac16f4351a3f3fcf36eb0e8e4d522fMD58open accessTHUMBNAILWOS000383231100005.pdf.jpgWOS000383231100005.pdf.jpgIM Thumbnailimage/jpeg6212${dspace.ui.url}/bitstream/11600/57446/10/WOS000383231100005.pdf.jpg293276ea9a668ef52ac52799c0d37510MD510open access11600/574462023-06-05 19:27:04.155open accessoai:repositorio.unifesp.br:11600/57446Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-06-05T22:27:04Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
A conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensis |
title |
A conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensis |
spellingShingle |
A conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensis Chaves, Alison F. A. [UNIFESP] dimorphism histidine kinase phosphorelay Paracoccidioides |
title_short |
A conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensis |
title_full |
A conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensis |
title_fullStr |
A conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensis |
title_full_unstemmed |
A conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensis |
title_sort |
A conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensis |
author |
Chaves, Alison F. A. [UNIFESP] |
author_facet |
Chaves, Alison F. A. [UNIFESP] Navarro, Marina V. [UNIFESP] Castilho, Daniele G. [UNIFESP] Calado, Juliana C. P. [UNIFESP] Conceicao, Palloma M. [UNIFESP] Batista, Wagner L. [UNIFESP] |
author_role |
author |
author2 |
Navarro, Marina V. [UNIFESP] Castilho, Daniele G. [UNIFESP] Calado, Juliana C. P. [UNIFESP] Conceicao, Palloma M. [UNIFESP] Batista, Wagner L. [UNIFESP] |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Chaves, Alison F. A. [UNIFESP] Navarro, Marina V. [UNIFESP] Castilho, Daniele G. [UNIFESP] Calado, Juliana C. P. [UNIFESP] Conceicao, Palloma M. [UNIFESP] Batista, Wagner L. [UNIFESP] |
dc.subject.eng.fl_str_mv |
dimorphism histidine kinase phosphorelay Paracoccidioides |
topic |
dimorphism histidine kinase phosphorelay Paracoccidioides |
description |
Paracoccidioides brasiliensis and P. lutzii, thermally dimorphic fungi, are the causative agents of paracoccidioidomycosis (PCM). Paracoccidioides infection occurs when conidia or mycelium fragments are inhaled by the host, which causes the Paracoccidioides cells to transition to the yeast form. The development of disease requires conidia inside the host alveoli to differentiate into yeast cells in a temperature-dependent manner. We describe the presence of a two-component signal transduction system in P. brasiliensis, which we investigated by expression analysis of a hypothetical protein gene (PADG_07579) that showed high similarity with the dimorphism-regulating histidine kinase (DRK1) gene of Blastomyces dermatitidis and Histoplasma capsulatum. This gene was sensitive to environmental redox changes, which was demonstrated by a dose-dependent decrease in transcript levels after peroxide stimulation and a subtler decrease in transcript levels after NO stimulation. Furthermore, the higher PbDRK1 levels after treatment with increasing NaCl concentrations suggest that this histidine kinase can play a role as osmosensing. In the mycelium-yeast (M -> Y) transition, PbDRK1 mRNA expression increased 14-fold after 24 h incubation at 37A degrees C, consistent with similar observations in other virulent fungi. These results demonstrate that the PbDRK1 gene is differentially expressed during the dimorphic M -> Y transition. Finally, when P. brasiliensis mycelium cells were exposed to a histidine kinase inhibitor and incubated at 37A degrees C, there was a delay in the dimorphic M -> Y transition, suggesting that histidine kinases could be targets of interest for PCM therapy. |
publishDate |
2016 |
dc.date.issued.fl_str_mv |
2016 |
dc.date.accessioned.fl_str_mv |
2020-08-14T13:43:56Z |
dc.date.available.fl_str_mv |
2020-08-14T13:43:56Z |
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info:eu-repo/semantics/publishedVersion |
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dc.identifier.citation.fl_str_mv |
Fems Yeast Research. Oxford, v. 16, n. 5, p. -, 2016. |
dc.identifier.uri.fl_str_mv |
https://repositorio.unifesp.br/handle/11600/57446 http://dx.doi.org/10.1093/femsyr/fow047 |
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1567-1356 |
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WOS000383231100005.pdf |
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10.1093/femsyr/fow047 |
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Fems Yeast Research. Oxford, v. 16, n. 5, p. -, 2016. 1567-1356 WOS000383231100005.pdf 10.1093/femsyr/fow047 WOS:000383231100005 |
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https://repositorio.unifesp.br/handle/11600/57446 http://dx.doi.org/10.1093/femsyr/fow047 |
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Oxford Univ Press |
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Oxford Univ Press |
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