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Identification of novel GAPDH-derived antimicrobial peptides secreted by Saccharomyces cerevisiae and involved in wine microbial interactions

2014-01Journal article Restricted access
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dc.contributor.authorBranco, Patrícia
dc.contributor.authorFrancisco, Diana
dc.contributor.authorChambon, Christophe
dc.contributor.authorHébraud, Michel
dc.contributor.authorArneborg, Nils
dc.contributor.authorAlmeida, Maria Gabriela
dc.contributor.authorCaldeira, Jorge
dc.contributor.authorAlbergaria, Helena
dc.date.accessioned2017-05-30T15:29:24Z
dc.date.available2017-05-30T15:29:24Z
dc.date.issued2014-01
dc.description.abstractSaccharomyces cerevisiae plays a primordial role in alcoholic fermentation and has a vast worldwide application in the production of fuel-ethanol, food and beverages. The dominance of S. cerevisiae over other microbial species during alcoholic fermentations has been traditionally ascribed to its higher ethanol tolerance. However, recent studies suggested that other phenomena, such as microbial interactions mediated by killer-like toxins, might play an important role. Here we show that S. cerevisiae secretes antimicrobial peptides (AMPs) during alcoholic fermentation that are active against a wide variety of wine-related yeasts (e.g. Dekkera bruxellensis) and bacteria (e.g. Oenococcus oeni). Mass spectrometry analyses revealed that these AMPs correspond to fragments of the S. cerevisiae glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein. The involvement of GAPDH-derived peptides in wine microbial interactions was further sustained by results obtained in mixed cultures performed with S. cerevisiae single mutants deleted in each of the GAPDH codifying genes (TDH1-3) and also with a S. cerevisiae mutant deleted in the YCA1 gene, which codifies the apoptosis-involved enzyme metacaspase. These findings are discussed in the context of wine microbial interactions, biopreservation potential and the role of GAPDH in the defence system of S. cerevisiae.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationBranco, P., Francisco, D., Chambon, C. et al. Appl Microbiol Biotechnol (2014) 98: 843. doi:10.1007/s00253-013-5411-ypt_PT
dc.identifier.doi10.1007/s00253-013-5411-ypt_PT
dc.identifier.issn0175-7598
dc.identifier.issn1432-0614
dc.identifier.urihttp://hdl.handle.net/10400.26/18446
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherSpringerpt_PT
dc.relationPURIFICATION AND BIOCHEMICAL/MOLECULAR CHARACTERISATION OF ANTIMICROBIAL PEPTIDES AMPS PRODUCED BY SACCHAROMYCES CEREVISIAE STRAINS: EVALUATION OF THE AMPS MODE OF ACTION
dc.relation.publisherversionhttps://dx.doi.org/10.1007/s00253-013-5411-ypt_PT
dc.subjectAntimicrobial peptidespt_PT
dc.subjectWine microbial interactionspt_PT
dc.subjectAlcoholic fermentationpt_PT
dc.subjectBiopreservationpt_PT
dc.subjectMetacaspasespt_PT
dc.subjectGlyceraldehyde-3-phosphate dehydrogenasept_PT
dc.titleIdentification of novel GAPDH-derived antimicrobial peptides secreted by Saccharomyces cerevisiae and involved in wine microbial interactionspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitlePURIFICATION AND BIOCHEMICAL/MOLECULAR CHARACTERISATION OF ANTIMICROBIAL PEPTIDES AMPS PRODUCED BY SACCHAROMYCES CEREVISIAE STRAINS: EVALUATION OF THE AMPS MODE OF ACTION
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/COMPETE/PEst-C%2FEQB%2FLA0006%2F2013/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F89673%2F2012/PT
oaire.citation.endPage853pt_PT
oaire.citation.startPage843pt_PT
oaire.citation.titleApplied Microbiology and Biotechnologypt_PT
oaire.citation.volume98(2)pt_PT
oaire.fundingStreamCOMPETE
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
rcaap.embargofctPolítica de copyright do editorpt_PT
rcaap.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublicationcd557642-38c3-4c8e-85bd-bd0292607f3d
relation.isProjectOfPublication030deef5-ade6-4d07-a2ff-cb46daeebf3d
relation.isProjectOfPublication.latestForDiscoverycd557642-38c3-4c8e-85bd-bd0292607f3d

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