Phosphosite-specific regulation of the oxidative-stress response of Paracoccidioides brasiliensis: a shotgun phosphoproteomic analysis

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dc.citation.issue1
dc.citation.volume19
dc.contributor.authorChaves, Alison Felipe Alencar [UNIFESP]
dc.contributor.authorCastilho, Daniele Goncalves [UNIFESP]
dc.contributor.authorNavarro, Marina Valente [UNIFESP]
dc.contributor.authorOliveira, Ana K.
dc.contributor.authorSerrano, Solange M. T.
dc.contributor.authorTashima, Alexandre Keiji [UNIFESP]
dc.contributor.authorBatista, Wagner Luiz [UNIFESP]
dc.coverageAmsterdam
dc.date.accessioned2020-07-31T12:46:57Z
dc.date.available2020-07-31T12:46:57Z
dc.date.issued2017
dc.description.abstractParacoccidioides brasiliensis, a thermally dimorphic fungus, is the causative agent of paracoccidioidomycosis, a systemic mycosis that is widespread in Latin America. This fungus is a facultative intracellular pathogen able to survive and replicate inside non-activated macrophages. Therefore, the survival of P. brasiliensis inside the host depends on the ability to adapt to oxidative stress induced by immune cells, especially alveolar macrophages. For several years, reactive oxygen species (ROS) were only associated with pathological processes. Currently, a plethora of roles for ROS in cell signaling have emerged. We have previously reported that low ROS concentrations cause cell proliferation in the human pathogenic fungus P. brasiliensis. In the present report, we investigated the influence of phosphorylation events in that process. Using a mass spectrometry-based approach, we mapped 440 phosphorylation sites in 230 P. brasiliensis proteins and showed that phosphorylation at different sites determines fungal responses to oxidative stress, which are regulated by phosphatases and kinases activities. Furthermore, we present additional evidence for a functional two-component signal transduction system in P. brasiliensis. These findings will help us to understand the phosphorylation events involved in the oxidative stress response. (C) 2016 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.en
dc.description.affiliationUniv Fed Sao Paulo, Dept Microbiol Immunol & Parasitol, Sao Paulo, SP, Brazil
dc.description.affiliationInst Butantan, Ctr Toxins, Lab Appl Toxinol, Immune Response & Cell Signaling, Sao Paulo, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Biochem, Sao Paulo, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Pharmaceut Sci, Diadema, SP, Brazil
dc.description.affiliationUnifespDepartment of Microbiology, Immunology and Parasitology, Universidade Federal de São Paulo, São Paulo, SP, Brazil
dc.description.affiliationUnifespDepartment of Biochemistry, Universidade Federal de São Paulo, São Paulo, SP, Brazil
dc.description.affiliationUnifespDepartment of Pharmaceutical Sciences, Universidade Federal de São Paulo, Diadema, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)]
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIDCNPq: 471015/2011-3
dc.description.sponsorshipIDFAPESP: 2011/14392-2
dc.description.sponsorshipIDFAPESP: 2014/13961-1
dc.description.sponsorshipIDFAPESP: 2012/19321-9
dc.description.sponsorshipIDFAPESP: CeTICS-CEPID 2013/07467-1
dc.description.sponsorshipIDFAPESP: 2012/17530-0
dc.format.extent34-46
dc.identifierhttp://dx.doi.org/10.1016/j.micinf.2016.08.004
dc.identifier.citationMicrobes And Infection. Amsterdam, v. 19, n. 1, p. 34-46, 2017.
dc.identifier.doi10.1016/j.micinf.2016.08.004
dc.identifier.issn1286-4579
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/56479
dc.identifier.wosWOS:000392677400004
dc.language.isoeng
dc.publisherElsevier Science Bv
dc.relation.ispartofMicrobes And Infection
dc.rightsAcesso restrito
dc.subjectOxidative stressen
dc.subjectPost-translational modificationen
dc.subjectPhosphorylationen
dc.subjectParacoccidioides brasiliensisen
dc.titlePhosphosite-specific regulation of the oxidative-stress response of Paracoccidioides brasiliensis: a shotgun phosphoproteomic analysisen
dc.typeArtigo
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