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Structural and Functional Characterization of the Type Three Secretion System (T3SS) Needle of Pseudomonas aeruginosa

dc.rights.licenseopenen_US
dc.contributor.authorLOMBARDI, Charlotte
dc.contributor.authorTOLCHARD, James
dc.contributor.authorBOUILLOT, Stephanie
dc.contributor.authorSIGNOR, Luca
dc.contributor.authorGEBUS, Caroline
dc.contributor.authorLIEBL, David
dc.contributor.authorFENEL, Daphna
dc.contributor.authorTEULON, Jean-Marie
dc.contributor.authorBROCK, Juliane
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorPELLEQUER, Jean-Luc
dc.contributor.authorFAUDRY, Eric
dc.contributor.authorLOQUET, Antoine
dc.contributor.authorATTRÉE, Ina
dc.contributor.authorDESSEN, Andréa
dc.contributor.authorJOB, Viviana
dc.date.accessioned2019
dc.date.available2019
dc.date.issued2019
dc.identifier.issn1664-302Xen_US
dc.identifier.otherhttps://www.frontiersin.org/articles/10.3389/fmicb.2019.00573/full#supplementary-materialen_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/3829
dc.description.abstractEnThe type three secretion system (T3SS) is a macromolecular protein nano-syringe used by different bacterial pathogens to inject effectors into host cells. The extracellular part of the syringe is a needle-like filament formed by the polymerization of a 9-kDa protein whose structure and proper localization on the bacterial surface are key determinants for efficient toxin injection. Here, we combined in vivo, in vitro, and in silico approaches to characterize the Pseudomonas aeruginosa T3SS needle and its major component PscF. Using a combination of mutagenesis, phenotypic analyses, immunofluorescence, proteolysis, mass spectrometry, atomic force microscopy, electron microscopy, and molecular modeling, we propose a model of the P. aeruginosa needle that exposes the N-terminal region of each PscF monomer toward the outside of the filament, while the core of the fiber is formed by the C-terminal helix. Among mutations introduced into the needle protein PscF, D76A, and P47A/Q54A caused a defect in the assembly of the needle on the bacterial surface, although the double mutant was still cytotoxic on macrophages in a T3SS-dependent manner and formed filamentous structures in vitro. These results suggest that the T3SS needle of P. aeruginosa displays an architecture that is similar to that of other bacterial needles studied to date and highlight the fact that small, targeted perturbations in needle assembly can inhibit T3SS function. Therefore, the T3SS needle represents an excellent drug target for small molecules acting as virulence blockers that could disrupt pathogenesis of a broad range of bacteria.
dc.language.isoENen_US
dc.subject.entype III secretion system
dc.subject.enPseudomonas aeruginosa
dc.subject.enT3SS needle
dc.subject.enstructure
dc.subject.envirulence
dc.subject.enimmunofluorescence microscopy
dc.subject.enmutagenesis
dc.title.enStructural and Functional Characterization of the Type Three Secretion System (T3SS) Needle of Pseudomonas aeruginosa
dc.title.alternativeFront. Microbiol.en_US
dc.typeArticle de revueen_US
dc.identifier.doi10.3389/fmicb.2019.00573
dc.subject.halChimie/Matériauxen_US
bordeaux.journalFrontiers in Microbiologyen_US
bordeaux.page573en_US
bordeaux.volume10en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03181980
hal.version1
hal.date.transferred2021-03-26T08:21:33Z
hal.exporttrue
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