Crystal structure of the C‐terminal domain of the <i>Salmonella</i> type III secretion system export apparatus protein InvA

Worrall, L.J.; Vuckovic, M.; Strynadka, N.C.J.

doi:10.1002/pro.382

Cited by 70 publications

(80 citation statements)

References 28 publications

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“…As shown in Fig. 2B, TRAF6 ubiquitination was strictly dependent on the T3SS, since TRAF6 ubiquitination was abolished in S. Typhimurium ΔinvA, a T3SS-defective mutant (23), in contrast to WT S. Typhimurium. Since we showed previously that SopB interacts directly with TRAF6 (11), we reasoned that SopB may be responsible for TRAF6 ubiquitination.…”

Section: Resultsmentioning

confidence: 71%

Tumor Necrosis Factor Receptor-Associated Factor 6 (TRAF6) Mediates Ubiquitination-Dependent STAT3 Activation upon Salmonella enterica Serovar Typhimurium Infection

et al. 2017

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Salmonella enterica serovar Typhimurium can inject effector proteins into host cells via type III secretion systems (T3SSs). These effector proteins modulate a variety of host transcriptional responses to facilitate bacterial growth and survival. Here we show that infection of host cells with S. Typhimurium specifically induces the ubiquitination of tumor necrosis factor receptor-associated factor 6 (TRAF6). This TRAF6 ubiquitination is triggered by the Salmonella pathogenicity island 1 (SPI-1) T3SS effectors SopB and SopE2. We also demonstrate that TRAF6 is involved in the SopB/ SopE2-induced phosphorylation of signal transducer and activator of transcription 3 (STAT3), a signaling event conducive to the intracellular growth of S. Typhimurium. Specifically, TRAF6 mediates lysine-63 ubiquitination within the Src homology 2 (SH2) domain of STAT3, which is an essential step for STAT3 membrane recruitment and subsequent phosphorylation in response to S. Typhimurium infection. TRAF6 ubiquitination participates in STAT3 phosphorylation rather than serving as only a hallmark of E3 ubiquitin ligase activation. Our results reveal a novel strategy in which S. Typhimurium T3SS effectors broaden their functions through the activation of host proteins in a ubiquitination-dependent manner to manipulate host cells into becoming a Salmonella-friendly zone.KEYWORDS Salmonella enterica serovar Typhimurium, TRAF6, ubiquitination, STAT3, Salmonella effectors I nfection with bacterial pathogens often induces host inflammatory responses (1), which are initiated by the recognition of microbial products, collectively known as pathogen-associated molecular patterns (PAMPs). PAMPs are recognized by Toll-like receptors (TLRs) or cytosolic NOD-like receptors (NLRs) (1, 2), which activate nuclear factor B (NF-B) and mitogen-activated protein kinases (MAPKs) and induce the production of proinflammatory cytokines critical for host defenses (3, 4). To overcome host defenses, some pathogens have developed strategies to dampen the host innate immune response by inactivating MAPKs or NF-B signaling. For instance, the Shigella flexneri phosphothreonine lyase OspF, which is injected into host cells by a type III secretion system (T3SS), inactivates the innate immune response by dephosphorylating MAPKs (5). The Yersinia protein YopJ/YopP, a T3SS effector protein containing both

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Section: Resultsmentioning

confidence: 71%

Tumor Necrosis Factor Receptor-Associated Factor 6 (TRAF6) Mediates Ubiquitination-Dependent STAT3 Activation upon Salmonella enterica Serovar Typhimurium Infection

et al. 2017

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“…[49,51,61]. Bacterial type III secretion systems evolved by multiple horizontal transfer systems [62] and invA is a prominent inner membrane component of Salmonella type III secretion system (T3SS) apparatus [63]. These lateral transfers have effectively changed the pathogenic characters of bacterial species [64].…”

Section: Resultsmentioning

confidence: 99%

Genetic diversity of food originated Salmonella isolates

Karatuğ

Yüksel

Akçelik

et al. 2018

Biotechnology & Biotechnological Equipment

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Currently, Salmonella enterica is the most common bacterial foodborne pathogen, causing serious extraintestinal disease. Typing methods play an important role on pathogens' source tracking, knowing the source(s) of bacteria in pharmaceutical sciences, preventing and controlling the diarrhea and food-poisoning outbreaks. The purpose of this study is to use different moleculer typing methods to determine the genetic variability of 38 foodborne Salmonella isolates that were previously identified by biochemical tests. The methods were evaluated by four molecular techniques including 16S rRNA sequencing, PFGE, PCR-RFLP and invA-spvC PCR. 16S rRNA sequencing results showed that four of the 38 isolates were Escherichia coli, Proteus mirabilis and Citrobacter murliniae, and the others were Salmonella enterica. Thirty-eight strains were subtyped by XbaI-PFGE into 20 profiles with different clusters, while they were subtyped by 16S rRNA-RFLP into 9 profiles with a single cluster. Out of two Salmonella isolates, the invasion gene (invA) was detected in all other Salmonella isolates (94%) and the virulence gene (spvC) was detected in 11% of Salmonella isolates. Our results suggested that the PFGE subtyping is the prominent method for the evaluation and benchmarking of molecular subtyping.

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“…Notably, several of these core T3SS components are structurally similar to components of F/V-type ATPases; most significantly, the ATPase FliI/SctN, the central stalk FliJ/ SctO and the negative regulator FliH/SctL resemble the a/b subunits, the g subunit and the b/d subunits of the F 0 F 1 -ATP synthase, respectively [33,[35][36][37] (figure 1). Assuming that the T3SS ATPase itself does not rotate, this suggests that the FliJ/SctO stalk might rotate and be linked to substrate export [29,33].…”

Section: Structural and Functional Homologies Among The T3ss And Othementioning

confidence: 99%

Type III secretion systems: the bacterial flagellum and the injectisome

Diepold

Armitage

2015

Phil. Trans. R. Soc. B

185

175

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One contribution of 12 to a theme issue 'The bacterial cell envelope'. The flagellum and the injectisome are two of the most complex and fascinating bacterial nanomachines. At their core, they share a type III secretion system (T3SS), a transmembrane export complex that forms the extracellular appendages, the flagellar filament and the injectisome needle. Recent advances, combining structural biology, cryo-electron tomography, molecular genetics, in vivo imaging, bioinformatics and biophysics, have greatly increased our understanding of the T3SS, especially the structure of its transmembrane and cytosolic components, the transcriptional, post-transcriptional and functional regulation and the remarkable adaptivity of the system. This review aims to integrate these new findings into our current knowledge of the evolution, function, regulation and dynamics of the T3SS, and to highlight commonalities and differences between the two systems, as well as their potential applications.

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Crystal structure of the C‐terminal domain of the Salmonella type III secretion system export apparatus protein InvA

Cited by 70 publications

References 28 publications

Tumor Necrosis Factor Receptor-Associated Factor 6 (TRAF6) Mediates Ubiquitination-Dependent STAT3 Activation upon Salmonella enterica Serovar Typhimurium Infection

Tumor Necrosis Factor Receptor-Associated Factor 6 (TRAF6) Mediates Ubiquitination-Dependent STAT3 Activation upon Salmonella enterica Serovar Typhimurium Infection

Genetic diversity of food originated Salmonella isolates

Type III secretion systems: the bacterial flagellum and the injectisome

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