Pseudomonas aeruginosa ExoS and ExoT

Barbieri, Joseph T.; Sun, Jianjun

doi:10.1007/s10254-004-0031-7

Cited by 211 publications

(218 citation statements)

References 62 publications

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“…The expression of a type-III secretion system (T3SS) by P. aeruginosa and T3SS-and T6SS-secreted effector proteins have been reported to be required for the cellular invasion and are supposed to influence the growthphase dependent cellular uptake of P. aeruginosa (11,(42)(43)(44)(45). However, our data suggest that initial membrane curvature and wrapping of the bacterium by the host PM depends neither on a bacterial secretion system nor on secreted effector proteins.…”

Section: Discussionmentioning

confidence: 65%

A lipid zipper triggers bacterial invasion

Eierhoff

Bastian

Thuenauer

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

128

161

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Significance Entry of bacteria into host cells critically depends on their proper engulfment by the plasma membrane. So far, actin polymerization has been described as a major driving force in this process. However, our study reveals that the interaction of the bacterial surface lectin LecA with the host cell glycosphingolipid Gb3 is fully sufficient to promote engulfment of Pseudomonas aeruginosa , whereas actin polymerization is dispensable. Hence, the formation of a “lipid zipper” represents a previously unidentified mechanism of bacterial uptake and demonstrates that bacterial pathogens have evolved lipid-based invasion strategies that may function in addition to protein receptor-based ones. Furthermore, by identifying the LecA/Gb3 interaction as the major invasion-promoting factor, our study provides new targets for drugs that may prevent bacterial invasion and dissemination.

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Section: Discussionmentioning

confidence: 65%

A lipid zipper triggers bacterial invasion

Eierhoff

Bastian

Thuenauer

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

128

161

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“…The highest specificity for RhoA, B, and C was observed with C3cer (Wilde et al 2003). The asparagine modification is a unique property of C3 toxins, since many bacterial ADP-ribosyltransferases modify arginine residues (e.g., cholera toxin, Pseudomonas exoenzyme S and T, C. botulinum C2 toxin; Moss and Vaughan 1977;Barbieri and Sun 2004;Vandekerckhove et al 1988) or a cysteine residue (e.g., pertussis toxin; West et al 1985). Recently, it was shown that the three isoforms C3stau1, 2, and 3 of Staphylococcus aureus differ in their substrate specificity.…”

Section: Introductionmentioning

confidence: 99%

C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins

Vogelsgesang

Pautsch

Aktories

2006

Naunyn-Schmied Arch Pharmacol

102

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The family of C3-like exoenzymes comprises seven bacterial ADP-ribosyltransferases of different origin. The common hallmark of these exoenzymes is the selective N-ADP-ribosylation of the low molecular mass GTPbinding proteins RhoA, B, and C and inhibition of signal pathways controlled by Rho GTPases. Therefore, C3-like exoenzymes were applied as pharmacological tools for analyses of cellular functions of Rho protein in numerous studies. Recent structural and functional analyses of C3-like exoenzymes provide detailed information on the molecular mechanisms and functional consequences of ADP-ribosylation catalyzed by these toxins. More recently additional non-enzymatic actions of C3-like ADP-ribosyltransferases have been identified showing that C3 transferases from Clostridium botulinum and Clostridium limosum form a GDI-like complex with the Ras-like low molecular mass GTPase Ral without ADP-ribosylation. These results add novel information on the molecular mode of action(s) of C3-like exoenzymes and are discussed in this review.

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“…It secretes four toxins by a TTSS: ExoS, ExoT, ExoU and ExoY (Barbieri & Sun, 2004;FinckBarbancon et al, 1997;Frank, 1997;Hauser et al, 1998;Yahr et al, 1996Yahr et al, , 1998. ExoS can induce a cytotoxic effect (Olson et al, 1999), and is associated with the ability to produce lung damage and poor outcome from P. aeruginosa infection (Roy-Burman et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

“…The GAP domain of ExoS had no effect on DNA synthesis. Many targets of the ExoS ADPRT domain action have been identified, including members of the small GTPase family proteins, such as Ras, Rab, Ral and Rap, as well as vimentin, and the GAP domain within its own N-terminal region Barbieri & Sun, 2004). These studies have demonstrated the effects of ExoS on the activation and interaction of small GTPases with downstream effectors.…”

Section: Introductionmentioning

confidence: 99%

Effects of the type III secreted pseudomonal toxin ExoS in the yeast Saccharomyces cerevisiae

Stirling

Evans

2006

Microbiology

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Pseudomonas aeruginosa secretes a number of toxins by a type III system, and these are important in virulence. One of them, ExoS, is a bifunctional toxin, with a GTPase-activating protein domain, as well as ADP ribosyltransferase (ADPRT) activity. These two domains have numerous potential cellular targets, but the overall mechanism of ExoS action remains unclear. The effects of ExoS in a simple eukaryotic system, the yeast Saccharomyces cerevisiae, using a tetracycline-regulated expression system were studied. This system allowed controlled expression of ExoS in yeast, which was not possible using a galactose-induced system. ExoS was found to be an extremely potent inhibitor of yeast growth, and to be largely dependent on the activity of its ADPRT domain. ExoS produced a dramatic alteration in actin distribution, with the appearance of large aggregates of cortical actin, and thickened disorganized cables, entirely dependent on the ADPRT domain. This phenotype is suggestive of actin stabilization, which was verified by showing that the cortical aggregates of actin induced by ExoS were resistant to treatment with latrunculin A, an agent that prevents actin polymerization. ExoS increased the numbers of mating projections produced following growth arrest with mating pheromone, and prevented subsequent DNA replication, an effect that is again dependent on the ADPRT domain. Following pheromone removal, ExoS produced altered development of the mating projections, which became elongated with a swollen bud-like tip. These results suggest alternative pathways for ExoS action in eukaryotic cells that may result from activation of small GTPases, and this yeast expression system is well suited to explore these pathways.

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Pseudomonas aeruginosa ExoS and ExoT

Cited by 211 publications

References 62 publications

A lipid zipper triggers bacterial invasion

A lipid zipper triggers bacterial invasion

C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins

Effects of the type III secreted pseudomonal toxin ExoS in the yeast Saccharomyces cerevisiae

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