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  4. DMO - Artigos de periódicos
Use este identificador para citar ou linkar para este item: https://ri.ufs.br/jspui/handle/riufs/25081
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dc.contributor.authorJacob, Tiago Rinaldi-
dc.contributor.authorPeres, Nalu Teixeira de Aguiar-
dc.contributor.authorMartins, Maíra Pompeu-
dc.contributor.authorLang, Elza Akie Sakamoto-
dc.contributor.authorSanches, Pablo Rodrigo-
dc.contributor.authorRossi Filho, Antonio-
dc.contributor.authorMartinez-Rossi, Nilce Maria-
dc.date.accessioned2026-07-06T18:20:51Z-
dc.date.available2026-07-06T18:20:51Z-
dc.date.issued2015-11-
dc.identifier.citationJACOB, T. R. et al. Heat shock protein 90 (Hsp90) as a molecular target for the development of novel drugs against the dermatophyte Trichophyton rubrum. Frontiers in Microbiology, Lausanne, v. 6, n. 1241, nov. 2015. Disponível em: https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2015.01241/full. Acesso em: 10 abr. 2026.pt_BR
dc.identifier.issn1664-302X-
dc.identifier.urihttps://ri.ufs.br/jspui/handle/riufs/25081-
dc.languageengpt_BR
dc.publisherFrontiers Media S. A.pt_BR
dc.relation.ispartofFrontiers in Microbiologypt_BR
dc.subjectHspeng
dc.subjectAntifungal therapyeng
dc.subjectMolecular targeteng
dc.subjectDrug synergismeng
dc.subjectItraconazoleeng
dc.subjectMicafungineng
dc.subject17-AAGeng
dc.titleHeat shock protein 90 (Hsp90) as a molecular target for the development of novel drugs against the dermatophyte Trichophyton rubrumpt_BR
dc.typeArtigopt_BR
dc.identifier.licenseCreative Commons Atribuição 4.0 Internacional (CC BY 4.0)pt_BR
dc.description.resumoTreatment of fungal infections is difficult due to several reasons, such as side effects of drugs, emergence of resistant strains, and limited number of molecular targets for the drug compounds. In fungi, heat shock proteins (Hsps) have been implicated in several processes with the conserved molecular chaperone Hsp90 emerging as a potential target for antifungal therapy. It plays key cellular roles by eliciting molecular response to environmental changes, morphogenesis, antifungal resistance, and fungal pathogenicity. Here, we evaluated the transcription profiles of hsp genes of the most prevalent dermatophyte Trichophyton rubrum in response to different environmental challenges including nutrient availability, interaction with cells and molecules of the host tissue, and drug exposure. The results suggest that each Hsp responds to a specific stress condition and that the cohort of Hsps facilitates fungal survival under various environmental challenges. Chemical inhibition of Hsp90 resulted in increased susceptibility of the fungus to itraconazole and micafungin, and decreased its growth in human nails in vitro. Moreover, some hsp and related genes were modulated by Hsp90 at the transcriptional level. We are suggesting a role of Hsp90 in the pathogenicity and drug susceptibility of T. rubrum as well as the regulation of other Hsps. The synergism observed between the inhibition of Hsp90 and the effect of itraconazole or micafungin in reducing the fungal growth is of great interest as a novel and potential strategy to treat dermatophytoses.pt_BR
dc.description.localLausannept_BR
dc.identifier.doihttps://doi.org/10.3389/fmicb.2015.01241-
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