Utilize este identificador para referenciar este registo: https://hdl.handle.net/10216/136357
Registo completo
Campo DCValorIdioma
dc.creatorTerceti, M
dc.creatorVences, A
dc.creatorMatanza, X
dc.creatorBarca, A
dc.creatorNoia, M
dc.creatorLisboa, J
dc.creatorSantos, NMS
dc.creatorVale, A
dc.creatorOsorio, C
dc.date.accessioned2021-09-20T10:53:26Z-
dc.date.available2021-09-20T10:53:26Z-
dc.date.issued2019
dc.identifier.issn1664-302X
dc.identifier.urihttps://hdl.handle.net/10216/136357-
dc.description.abstractThe RstB histidine kinase of the two component system RstAB positively regulates the expression of damselysin (Dly), phobalysin P (PhlyP) and phobalysin C (PhlyC) cytotoxins in the fish and human pathogen Photobacterium damselae subsp. damselae, a marine bacterium of the family Vibrionaceae. However, the function of the predicted cognate response regulator RstA has not been studied so far, and the role of the RstAB system in other cell functions and phenotypes remain uninvestigated. Here, we analyzed the effect of rstA and rstB mutations in cell fitness and in diverse virulence-related features. Both rstA and rstB mutants were severely impaired in virulence for sea bream and sea bass fish. Mutants in rstA and rstB genes were impaired in hemolysis and in Dly-dependent phospholipase activity but had intact PlpV-dependent phospholipase and ColP-dependent gelatinase activities. rstA and rstB mutants grown at 0.5% NaCl exhibited impaired swimming motility, enlarged cell size and impaired ability to separate after cell division, whereas at 1% NaCl the mutants exhibited normal phenotypes. Mutation of any of the two genes also impacted tolerance to benzylpenicillin. Notably, rstA and rstB mutants showed impaired secretion of a number of type II secretion system (T2SS)-dependent proteins, which included the three major cytotoxins Dly, PhlyP and PhlyC, as well as a putative delta-endotoxin and three additional uncharacterized proteins which might constitute novel virulence factors of this pathogenic bacterium. The analysis of the T2SS-dependent secretome of P. damselae subsp. damselae also led to the identification of RstAB-independent potential virulence factors as lipoproteins, sialidases and proteases. The RstAB regulon included plasmid, chromosome I and chromosome II-encoded genes that showed a differential distribution among isolates of this subspecies. This study establishes RstAB as a major regulator of virulence and diverse cellular functions in P. damselae subsp. damselae.
dc.description.sponsorshipThis work has been supported by grant AGL2016-79738-R (AEI/FEDER, EU) from the State Agency for Research (AEI) of Spain, and co-funded by the FEDER Programme from the European Union. The support of Xunta de Galicia (Spain) with grant ED431C 2018/18 is also acknowledged. MT thanks the Brazilian Ministry of Education and CAPES (Coordenaçao de Aperfeiçoamento de Pessoal de Nível Superior) for a predoctoral fellowship. XM thanks Xunta de Galicia for a predoctoral fellowship. AdV was supported by the FCT fellowship SFRH/BPD/95777/2013. The mass spectrometry technique was performed at the Proteomics i3S Scientific Platform with the assistance of Hugo Osório. This work had support from the Portuguese Mass Spectrometry Network, integrated in the National Roadmap of Research Infrastructures of Strategic Relevance (ROTEIRO/0028/2013; LISBOA-01-0145-FEDER-022125).
dc.language.isoeng
dc.publisherFrontiers Media
dc.relation.ispartofFrontiers in Microbiology, vol.10:897
dc.rightsopenAccess
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectCarSR
dc.subjectDamselysin
dc.subjectPhobalysin
dc.subjectPhotobacterium damselae
dc.subjectRstAB
dc.subjectT2SS
dc.subjectTCS
dc.titleThe RstAB system impacts virulence, motility, cell morphology, penicillin tolerance and production of type II secretion system-dependent factors in the fish and human pathogen photobacterium damselae subsp. damselae
dc.typeArtigo em Revista Científica Internacional
dc.contributor.uportoInstituto de Investigação e Inovação em Saúde
dc.identifier.doi10.3389/fmicb.2019.00897
dc.relation.publisherversionhttps://www.frontiersin.org/articles/10.3389/fmicb.2019.00897/full
Aparece nas coleções:I3S - Artigo em Revista Científica Internacional

Ficheiros deste registo:
Ficheiro Descrição TamanhoFormato 
10.3389-fmicb.2019.00897.pdf5.1 MBAdobe PDFThumbnail
Ver/Abrir


Este registo está protegido por Licença Creative Commons Creative Commons