Txc, a New Type II Secretion System of Pseudomonas aeruginosa Strain PA7, Is Regulated by the TtsS/TtsR Two-Component System and Directs Specific Secretion of the CbpE Chitin-Binding Protein

Cadoret, F.; Ball, Geneviève; Douzi, Badreddine; Voulhoux, Romé

doi:10.1128/jb.01563-14

Cited by 30 publications

(25 citation statements)

References 66 publications

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“…Xcp and Hxc complexes are present and functional in PA7 (Cadoret et al, 2014). The main effector of Xcp is exotoxin A (ToxA), a potent inhibitor of protein translation in the host.…”

Section: Synonymsmentioning

confidence: 99%

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Pseudomonas aeruginosa renews its virulence factors

Huber

Basso

Reboud

et al. 2016

Environ Microbiol Rep

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Highly divergent strains of the major human opportunistic pathogen Pseudomonas aeruginosa have been isolated around the world by different research laboratories. They came from patients with various types of infectious diseases or from the environment. These strains are devoid of the major virulence factor used by classical strains, the Type III secretion system, but possess additional putative virulence factors, including a novel two-partner secretion system, ExlBA, responsible for the hypervirulent behavior of some clinical isolates. Here, we review the genetic and phenotypic characteristics of these recently-discovered P. aeruginosa outliers.

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“…Xcp and Hxc complexes are present and functional in PA7 (Cadoret et al, 2014). The main effector of Xcp is exotoxin A (ToxA), a potent inhibitor of protein translation in the host.…”

Section: Synonymsmentioning

confidence: 99%

“…A third T2SS has been identified in PA7, called Txc for third homolog for Xcp (Cadoret et al, 2014). A cluster of 14 genes, including 11 'core' genes (txcP to txcZ or PSPA7_1417 to PSPA7_1407), a secreted substrate (cbpE or PA7_1419) and a regulatory protein (ttsS or PSPA7_1420) have been identified in a region of genome plasticity (RGP69).…”

Section: Synonymsmentioning

confidence: 99%

Pseudomonas aeruginosa renews its virulence factors

Huber

Basso

Reboud

et al. 2016

Environ Microbiol Rep

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“…Pseudomonas aeruginosa , an opportunistic pathogen of major importance in cystic fibrosis patients, contains two distinct T2SS machineries (Ball et al, 2002; Jyot et al, 2011) and in certain strains even three (Cadoret et al, 2014);…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspL

Lü

Korotkov

Hól

2014

Journal of Structural Biology

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The type II secretion system (T2SS) is present in many Gram-negative bacteria and is responsible for secreting a large number of folded proteins, including major virulence factors, across the outer membrane. The T2SS consists of 11-15 different proteins most of which are present in multiple copies in the assembled secretion machinery. The ATPase GspE, essential for the functioning of the T2SS, contains three domains (N1E, N2E and CTE) of which the N1E domain is associated with the cytoplasmic domain of the inner membrane protein GspL Here we describe and analyze the structure of the GspE•cyto-GspL complex from Vibrio vulnificus in the presence of an ATP analog, AMPPNP. There are three such ∼83 kDa complexes per asymmetric unit with essentially the same structure. The N2E and CTE domains of a single V. vulnificus GspE subunit adopt a mutual orientation that has not been seen before in any of the previous GspE structures, neither in structures of related ATPases from other secretion systems. This underlines the tremendous conformational flexibility of the T2SS secretion ATPase. Cyto-GspL interacts not only with the N1E domain, but also with the CTE domain and is even in contact with AMPPNP. Moreover, the cyto-GspL domains engage in two types of mutual interactions, resulting in two essentially identical, but crystallographically independent, “cyto-GspL rods” that run throughout the crystal. Very similar rods are present in previous crystals of cyto-GspL and of the N1E•cyto-GspL complex. This arrangement, now seen four times in three entirely different crystal forms, involves contacts between highly conserved residues suggesting a role in the biogenesis or the secretion mechanism or both of the T2SS.

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“…However, in a cystic fibrosis context, colonizing strains modulate levels of expression of some of these virulence factors (Hauser et al , 2011), namely down‐regulation of the T3SS (Jain et al , 2004) and undergo a remarkable accumulation of pathoadaptive mutations (Marvig et al , 2014). The PA7‐related P. aeruginosa strains lack the 20‐Kb‐long genomic region encoding the T3SS core components and all genes encoding secreted effectors but contains several additional genomic islands and potential novel virulence factors (Pirnay et al , 2009; Roy et al , 2010; Cadoret et al , 2014; Freschi et al , 2015). In some of these strains, such as CLJ1, an exolysin secreted by a two‐partner secretion system is responsible for hypervirulence (Elsen et al , 2014).…”

Section: Discussionmentioning

confidence: 99%

“…DNA product was then cloned by the SLIC method (Jeong et al , 2012) into pKNG208 (Cadoret et al , 2014) digested by Apa I/ Spe I to generate pKNG208‐ pumA::bla1 vector.…”

Section: Methodsmentioning

confidence: 99%

A Pseudomonas aeruginosa TIR effector mediates immune evasion by targeting UBAP1 and TLR adaptors

et al. 2017

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Bacterial pathogens often subvert the innate immune system to establish a successful infection. The direct inhibition of downstream components of innate immune pathways is particularly well documented but how bacteria interfere with receptor proximal events is far less well understood. Here, we describe a Toll/interleukin 1 receptor (TIR) domain‐containing protein (PumA) of the multi‐drug resistant Pseudomonas aeruginosa PA7 strain. We found that PumA is essential for virulence and inhibits NF‐κB, a property transferable to non‐PumA strain PA14, suggesting no additional factors are needed for PumA function. The TIR domain is able to interact with the Toll‐like receptor (TLR) adaptors TIRAP and MyD88, as well as the ubiquitin‐associated protein 1 (UBAP1), a component of the endosomal‐sorting complex required for transport I (ESCRT‐I). These interactions are not spatially exclusive as we show UBAP1 can associate with MyD88, enhancing its plasma membrane localization. Combined targeting of UBAP1 and TLR adaptors by PumA impedes both cytokine and TLR receptor signalling, highlighting a novel strategy for innate immune evasion.

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Txc, a New Type II Secretion System of Pseudomonas aeruginosa Strain PA7, Is Regulated by the TtsS/TtsR Two-Component System and Directs Specific Secretion of the CbpE Chitin-Binding Protein

Cited by 30 publications

References 66 publications

Pseudomonas aeruginosa renews its virulence factors

Pseudomonas aeruginosa renews its virulence factors

Crystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspL

A Pseudomonas aeruginosa TIR effector mediates immune evasion by targeting UBAP1 and TLR adaptors

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