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Sphingolipid domains in the plasma membrane of fungal cells : Interplay with membrane proteins and antifungal resistance

2023-01Doctoral thesis Open access
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datacite.subject.fosCiências Naturais::Ciências Biológicaspt_PT
dc.contributor.advisorAlmeida, Rodrigo F. M. de
dc.contributor.authorSantos, Filipa C.
dc.date.accessioned2023-06-01T14:40:24Z
dc.date.available2023-06-01T14:40:24Z
dc.date.issued2023-01
dc.date.submitted2022-08
dc.description.abstractPlasma membrane (PM) carries out multiple functions a tightly regulated dynamic organization into specialized domains of different size, stability, and composition. Sphingolipids are a major class of lipids of PM being crucial for its structure and function. A specific type of ergosterol-depleted PM domains in fungi, where lipids are tightly packed in a very rigid gel phase, comprises the sphingolipid-enriched domains (SLEDs). In this work, the presence of SLEDs in a mold, Neurospora crassa, was disclosed, as well as their involvement in the response to the antifungal staurosporine. A comparison with the budding yeast Saccharomyces cerevisiae was performed, taking into consideration the known differences between their PM sphingolipidomes. The studies with N. crassa were performed in conidial suspensions along different time points of conidial germination, using several fluorescence spectroscopy techniques and a multiprobe approach. S. cerevisiae living cells were studied in mi-exponential phase. To evaluate the impact of changing sphingolipid composition in the organization of the two main yeast PM compartments, MCC (arginine/ H+ symporter Can1p) and MCP (H+ ATPase Pma1p), the time-resolved fluorescence properties of Can1p tagged with GFP and Pma1p tagged with mRFP, respectively, were studied by FLIM in wt and a mutant strain with a different sphingolipid profile, ipt1∆. IPT1 deletion strongly affects the rigidity of gel domains and Pma1p PM distribution, whereas no significant alterations could be perceived neither in ergosterol-enriched domains nor Can1p distribution. Thus, this work strongly suggests that proper SLEDs hydrophobic chain packing is required for an adequate organization of the MCP, but not MCC. Finally, considering that the PM is crucial for antifungal action, a biophysical connection between SLEDs and antifungal activity was explored in S. cerevisiae.pt_PT
dc.identifier.tid101549008pt_PT
dc.identifier.urihttp://hdl.handle.net/10451/57798
dc.language.isoengpt_PT
dc.relationSphingolipid Organization in the Plasma Membrane of Saccharomyces cerevisiae. Implications for Yeast Membrane Compartments and Antifungal Resistance
dc.relationSphingolipid organization in the plasma membrane of Saccharomyces cerevisiae. Implication in antifungal mode of action and fungal resistance.
dc.relationCentro de Química Estrutural
dc.relationCenter of Chemistry and Biochemistry
dc.subjectmembrana plasmática de fungospt_PT
dc.subjectagentes antifúngicospt_PT
dc.subjectfluorescênciapt_PT
dc.subjectdomínios ricos em esfingolípidos (SLEDs)pt_PT
dc.subjectcompartimentos de membrana (MCC e MCP)pt_PT
dc.titleSphingolipid domains in the plasma membrane of fungal cells : Interplay with membrane proteins and antifungal resistancept_PT
dc.typedoctoral thesis
dspace.entity.typePublication
oaire.awardTitleSphingolipid Organization in the Plasma Membrane of Saccharomyces cerevisiae. Implications for Yeast Membrane Compartments and Antifungal Resistance
oaire.awardTitleSphingolipid organization in the plasma membrane of Saccharomyces cerevisiae. Implication in antifungal mode of action and fungal resistance.
oaire.awardTitleCentro de Química Estrutural
oaire.awardTitleCenter of Chemistry and Biochemistry
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/OE/SFRH%2FBD%2F108031%2F2015/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBBB-BQB%2F6071%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/EXPL%2FBIA-BFS%2F1034%2F2021/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F00100%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UID%2FMulti%2F00612%2F2013/PT
oaire.fundingStreamOE
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
person.familyNamePedro Costa Santos
person.givenNameFilipa
person.identifierJ-8627-2013
person.identifier.ciencia-idBE16-3628-D73B
person.identifier.orcid0000-0001-9632-2300
person.identifier.scopus-author-id55589595100
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typedoctoralThesispt_PT
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thesis.degree.nameTese de doutoramento, Bioquímica (Biofísica Molecular), Universidade de Lisboa, Faculdade de Ciências, 2023pt_PT

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