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Molecular architecture of bacterial amyloids in Bacillus biofilms

hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorEL MAMMERI, Nadia
dc.contributor.authorHIERREZUELO, Jesus
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorTOLCHARD, James
dc.contributor.authorCAMARA-ALMIRON, Jesus
dc.contributor.authorCARO-ASTORGA, Joaquin
dc.contributor.authorALVAREZ-MENA, Ana
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDUTOUR, Antoine
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBERBON, Melanie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorSHENOY, Jayakrishna
hal.structure.identifierInstitut Européen de Chimie et Biologie [IECB]
dc.contributor.authorMORVAN, Estelle
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGRELARD, Axelle
hal.structure.identifierInstitut Européen de Chimie et Biologie [IECB]
dc.contributor.authorKAUFFMANN, Brice
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLECOMTE, Sophie
dc.contributor.authorDE VICENTE, Antonio
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorROMERO, Diego
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
dc.date.accessioned2020-06-05T08:52:13Z
dc.date.available2020-06-05T08:52:13Z
dc.date.issued2019
dc.identifier.issn0892-6638en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/7754
dc.description.abstractEnThe formation of biofilms provides structural and adaptive bacterial response to the environment. In Bacillus species, the biofilm extracellular matrix is composed of exopolysaccharides, hydrophobins, and several functional amyloid proteins. We report, using multiscale approaches such as solid-state NMR (SSNMR), electron microscopy, X-ray diffraction, dynamic light scattering, attenuated total reflection Fourier transform infrared (FTIR), and immune-gold labeling, the molecular architecture of B. subtilis and pathogenic B. cereus functional amyloids. SSNMR data reveal that the major amyloid component TasA in its fibrillar amyloid form contain beta-sheet and alpha-helical secondary structure, suggesting a nontypical amyloid architecture in B. subtilis. Proteinase K digestion experiments indicate the amyloid moiety is 100 aa long, and subsequent SSNMR and FTIR signatures for B. subtilis and B. cereus TasA filaments highlight a conserved amyloid fold, albeit with substantial differences in structural polymorphism and secondary structure composition. Structural analysis and coassembly data on the accessory protein TapA in B. subtilis and its counterpart camelysin in B. cereus reveal a catalyzing effect between the functional amyloid proteins and a common structural architecture, suggesting a coassembly in the context of biofilm formation. Our findings highlight nontypical amyloid behavior of these bacterial functional amyloids, underlining structural variations between biofilms even in closely related bacterial species.-El Mammeri, N., Hierrezuelo, J., Tolchard, J., Camara-Almiron, J., Caro-Astorga, J., Alvarez-Mena, A., Dutour, A., Berbon, M., Shenoy, J., Morvan, E., Grelard, A., Kauffmann, B., Lecomte, S., de Vicente, A., Habenstein, B., Romero, D., Loquet, A. Molecular architecture of bacterial amyloids in Bacillus biofilms.
dc.language.isoENen_US
dc.subject.enfunctional amyloids
dc.subject.enextracellular matrix
dc.subject.ensolid‐state NMR
dc.title.enMolecular architecture of bacterial amyloids in Bacillus biofilms
dc.typeArticle de revueen_US
dc.identifier.doi10.1096/fj.201900831Ren_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalFASEB journalen_US
bordeaux.pagefj201900831R-fj201900831Ren_US
bordeaux.volume33en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.issue11en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.identifier.funderIDEuropean Research Councilen_US
hal.identifierhal-02412754
hal.version1
hal.date.transferred2020-09-15T07:25:53Z
hal.exporttrue
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