Please use this identifier to cite or link to this item: http://hdl.handle.net/10773/36908
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dc.contributor.authorCovas, Cláudiapt_PT
dc.contributor.authorAlmeida, Beatrizpt_PT
dc.contributor.authorEsteves, Ana Cristinapt_PT
dc.contributor.authorLourenço, Joanapt_PT
dc.contributor.authorDomingues, Pedropt_PT
dc.contributor.authorCaetano, Tâniapt_PT
dc.contributor.authorMendo, Sóniapt_PT
dc.date.accessioned2023-04-06T11:51:10Z-
dc.date.available2023-04-06T11:51:10Z-
dc.date.issued2021-01-25-
dc.identifier.issn1871-6784pt_PT
dc.identifier.urihttp://hdl.handle.net/10773/36908-
dc.description.abstractNovel natural products are urgently needed to address the worldwide incidence of bacterial resistance to antibiotics. Extreme environments are a major source of novel compounds with unusual chemical structures. Pedobacter lusitanus NL19 is a new bacterial species that was isolated from one such environment and which produces compounds with potent activity against relevant microorganisms in the clinical, food, veterinary and aquaculture areas. The production of antimicrobials by P. lusitanus NL19 was identified in tryptic soy agar (TSA), but not in its equivalent broth (TSB). It was observed that in TSB medium a high concentration of casein peptone (PC) repressed the production of antibacterial compounds. HPLC, MS and MS/MS spectra with de novo sequencing revealed that the bioactivity of P. lusitanus NL19 was due to the production of pedopeptins. Hence, biosynthesis of pedopeptins is inhibited by high concentrations of PC in the broth medium. Furthermore, a nonribosomal peptide synthetase (NRPS) gene cluster was identified in the genome of NL19 encoding the biosynthesis of the peptides. qPCR analysis confirmed that the transcription of these genes is repressed in cells cultivated in high concentrations of PC. It is shown that pedopeptins are nonribosomal peptides with a broad-spectrum activity, including against Gram-positive and Gram-negative bacteria and yeasts.pt_PT
dc.language.isoengpt_PT
dc.publisherElsevierpt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/FARH/SFRH%2FBD%2F98446%2F2013/PTpt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/FARH/SFRH%2FBPD%2F77900%2F2011/PTpt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/OE/SFRH%2FBPD%2F92554%2F2013/PTpt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/CEEC IND 2017/CEECIND%2F01463%2F2017%2FCP1459%2FCT0013/PTpt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F50017%2F2020/PTpt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F50017%2F2020/PTpt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UID%2FQUI%2F00062%2F2019/PTpt_PT
dc.relationLISBOA-01-0145-FEDER-402-022125pt_PT
dc.relationUID/MULTI/4279/2019pt_PT
dc.rightsopenAccesspt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/pt_PT
dc.subjectExtreme environmentspt_PT
dc.subjectAntimicrobial activitypt_PT
dc.subjectNRPSpt_PT
dc.subjectCasein peptonept_PT
dc.subjectqPCRpt_PT
dc.subjectPedopeptinspt_PT
dc.titlePeptone from casein, an antagonist of nonribosomal peptide synthesis: a case study of pedopeptins produced by Pedobacter lusitanus NL19pt_PT
dc.typearticlept_PT
dc.description.versionpublishedpt_PT
dc.peerreviewedyespt_PT
degois.publication.firstPage62pt_PT
degois.publication.lastPage71pt_PT
degois.publication.titleNew biotechnologypt_PT
degois.publication.volume60pt_PT
dc.identifier.doi10.1016/j.nbt.2020.07.006pt_PT
Appears in Collections:CESAM - Artigos
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