MapB, the Brucella suis TamB homologue, is involved in cell envelope biogenesis, cell division and virulence

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dc.citation.titleScientific Reports
dc.citation.volume9
dc.contributor.otherDe Bolle, Xavier: provide the anti-OMPs and anti-LPS antibodies
dc.contributor.otherUgalde, Juan: provide the anti-OMPs and anti-LPS antibodies
dc.contributor.otherCassataro, Juliana: provide the anti-OMPs and anti-LPS antibodies
dc.contributor.otherSpera, Juan Manuel: provide the PQE31-3xFLAG plasmid
dc.contributor.otherBravo, Marta: DNA sequencing
dc.creatorBialer, Magalí Graciela
dc.creatorRuiz-Ranwez, Verónica
dc.creatorSycz, Gabriela
dc.creatorEstein, Silvia Marcela
dc.creatorRusso, Daniela Marta
dc.creatorAltabe, Silvia Graciela
dc.creatorSieira, Rodrigo
dc.creatorZorreguieta, Ángeles
dc.date.accessioned2024-06-25T13:12:51Z
dc.date.available2024-06-25T13:12:51Z
dc.date.issued2019-02-15
dc.description.abstractBrucella species are Gram-negative, facultative intracellular pathogens responsible for a worldwide zoonosis. The envelope of Brucella exhibits unique characteristics that make these bacteria furtive pathogens and resistant to several host defence compounds. We have identified a Brucella suis gene (mapB) that appeared to be crucial for cell envelope integrity. Indeed, the typical resistance of Brucella to both lysozyme and the cationic lipopeptide polymyxin B was markedly reduced in a ∆mapB mutant. MapB turned out to represent a TamB orthologue. This last protein, together with TamA, a protein belonging to the Omp85 family, form a complex that has been proposed to participate in the translocation of autotransporter proteins across the outer membrane (OM). Accordingly, we observed that MapB is required for proper assembly of an autotransporter adhesin in the OM, as most of the autotransporter accumulated in the mutant cell periplasm. Both assessment of the relative amounts of other specific outer membrane proteins (OMPs) and a proteome approach indicated that the absence of MapB did not lead to an extensive alteration in OMP abundance, but to a reduction in the relative amounts of a protein subset, including proteins from the Omp25/31 family. Electron microscopy revealed that ∆mapB cells exhibit multiple anomalies in cell morphology, indicating that the absence of the TamB homologue in B. suis severely affects cell division. Finally, ∆mapB cells were impaired in macrophage infection and showed an attenuated virulence phenotype in the mouse model. Collectively, our results indicate that the role of B. suis TamB homologue is not restricted to participating in the translocation of autotransporters across the OM but that it is essential for OM stability and protein composition and that it is involved in cell envelope biogenesis, a process that is inherently coordinated with cell division.
dc.description.filFil: Bialer, Magalí Graciela. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET); Argentina.
dc.description.filFil: Ruiz-Ranwez, Verónica. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET); Argentina.
dc.description.filFil: Sycz, Gabriela. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET); Argentina.
dc.description.filFil: Estein, Silvia Marcela. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Centro de Investigación Veterinaria de Tandil (CIVETAN-CONICET); Argentina.
dc.description.filFil: Russo, Daniela Marta. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET); Argentina.
dc.description.filFil: Altabe, Silvia Graciela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET). Departamento de Microbiología; Argentina.
dc.description.filFil: Sieira, Rodrigo. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET); Argentina.
dc.description.filFil: Zorreguieta, Ángeles. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina.
dc.description.sponsorshipAgencia Nacional de Promoción de la Investigación, el Desarrollo Tecnológico y la Innovación (Agencia I+D+i): PICT 2012-2171 and PICT 2016-2722
dc.description.versionpeerreviewed
dc.format.extent1-18
dc.identifier.issn2045-2322
dc.identifier.urihttps://hdl.handle.net/2133/27340
dc.language.isoen
dc.publisherSpringer Nature
dc.relation.publisherversionhttps://doi.org/10.1038/s41598-018-37668-3
dc.relation.publisherversionhttps://www.nature.com/articles/s41598-018-37668-3
dc.rightsopenAccess
dc.rights.holderBialer, Magalí Graciela
dc.rights.holderRuiz-Ranwez, Verónica
dc.rights.holderSycz, Gabriela
dc.rights.holderEstein, Silvia Marcela
dc.rights.holderRusso, Daniela Marta
dc.rights.holderAltabe, Silvia Graciela
dc.rights.holderSieira, Rodrigo
dc.rights.holderZorreguieta, Ángeles
dc.rights.holderUniversidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas
dc.rights.textAttribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectMapB
dc.subjectBrucella suis
dc.subjectCell envelope biogenesis
dc.subjectTamB homologue
dc.subjectCell division
dc.subjectVirulence
dc.titleMapB, the Brucella suis TamB homologue, is involved in cell envelope biogenesis, cell division and virulence
dc.typearticulo
dc.type.versionpublishedVersion

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