An Inv/Mxi‐Spa‐like type III protein secretion system in <i>Burkholderia pseudomallei</i> modulates intracellular behaviour of the pathogen

Stevens, Mark P.; Wood, Michael W.; Taylor, Lowrie A.; Monaghan, Paul; Hawes, Philippa C.; Jones, Philip W.; Wallis, Timothy S.; Galyov, Edouard E.

doi:10.1046/j.1365-2958.2002.03190.x

Cited by 253 publications

(303 citation statements)

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“…Interestingly, Burkholderia spp. contain not only a SPI-1 T3S system but also Hrptype T3S systems that are usually specific for plant-pathogenic bacteria (449,522) (Fig. 1D).…”

Section: Variations On a Theme-differences And Similarities Of T3s Symentioning

confidence: 99%

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Büttner

2012

Microbiol Mol Biol Rev

359

482

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SUMMARY Flagellar and translocation-associated type III secretion (T3S) systems are present in most Gram-negative plant- and animal-pathogenic bacteria and are often essential for bacterial motility or pathogenicity. The architectures of the complex membrane-spanning secretion apparatuses of both systems are similar, but they are associated with different extracellular appendages, including the flagellar hook and filament or the needle/pilus structures of translocation-associated T3S systems. The needle/pilus is connected to a bacterial translocon that is inserted into the host plasma membrane and mediates the transkingdom transport of bacterial effector proteins into eukaryotic cells. During the last 3 to 5 years, significant progress has been made in the characterization of membrane-associated core components and extracellular structures of T3S systems. Furthermore, transcriptional and posttranscriptional regulators that control T3S gene expression and substrate specificity have been described. Given the architecture of the T3S system, it is assumed that extracellular components of the secretion apparatus are secreted prior to effector proteins, suggesting that there is a hierarchy in T3S. The aim of this review is to summarize our current knowledge of T3S system components and associated control proteins from both plant- and animal-pathogenic bacteria.

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“…Interestingly, Burkholderia spp. contain not only a SPI-1 T3S system but also Hrptype T3S systems that are usually specific for plant-pathogenic bacteria (449,522) (Fig. 1D).…”

Section: Variations On a Theme-differences And Similarities Of T3s Symentioning

confidence: 99%

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Büttner

2012

Microbiol Mol Biol Rev

359

482

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“…Among these bacteria is Salmonella typhimurium, which is one of the most common pathogens of food poisoning in the U.S. Salmonellosis contributes significantly to hospitalization and morbidity among susceptible individuals such as the elderly, children, and people with compromised immune systems caused by AIDS and chemotherapy. 1 Other pathogens that use a TTSA are Shigella flexneri (shigellosis), 2 Yersinia pestis (plague), 3 Burkholderia pseudomallei (melioidosis) 4 and Pseudomonas aeruginosa (pulmonary infections among cystic fibrosis patients). 5 No vaccines are currently approved for general use against any of these pathogens, and together *Corresponding author: rdguzman@ku.edu, Phone: (785) 864 4923.with the appearance of antibiotic resistant strains 6, 7 and the bioterrorism potential of B. pseudomallei, 8 these pathogens continue to pose major public health and safety concerns.…”

Section: Introductionmentioning

confidence: 99%

Differences in the Electrostatic Surfaces of the Type III Secretion Needle Proteins PrgI, BsaL, and MxiH

Wang

Ouellette

Egan

et al. 2007

Journal of Molecular Biology

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Gram-negative bacteria use a needle-like protein assembly, the type III secretion apparatus, to inject virulence factors into target cells to initiate human disease. The needle is formed by the polymerization of ~120 copies of a small acidic protein that is conserved among diverse pathogens. We previously reported the structure of the BsaL needle monomer from Burkholderia pseudomallei by nuclear magnetic resonance (NMR) spectroscopy and others have determined the crystal structure of the Shigella flexneri MxiH needle. Here, we report the NMR structure of the PrgI needle protein of Salmonella typhimurium, a human pathogen associated with food poisoning. PrgI, BsaL, and MxiH form similar two helix bundles, however, the electrostatic surfaces of PrgI differ radically from those of BsaL or MxiH. In BsaL and MxiH, a large negative area is on a face formed by the helix α 1 -α 2 interface. In PrgI, the major negatively charged surface is not on the "face" but instead is on the "side" of the two helix bundle, and only residues from helix α 1 contribute to this negative region. Despite being highly acidic proteins, these molecules contain large basic regions, suggesting that electrostatic contacts are important in needle assembly. Our results also suggest that needle packing interactions may be different among these bacteria and provide the structural basis for why PrgI and MxiH, despite 63% sequence identity, are not interchangeable in S. typhimurium and S. flexneri.

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“…B. pseudomallei possesses many virulence factors including three type III secretion systems (25). One of these loci designated the Burkholderia secretion apparatus (bsa) gene cluster shares homology with the Salmonella typhimurium inv/spa/prg T3SS and is required for cellular invasion and escape from endocytic vesicles (26). This bacterium also possesses six type VI secretion system (T6SS) clusters, and the T6SS-5 has been reported to be important for the invasion of macrophages (27).…”

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confidence: 99%

Suppression of Host Innate Immune Response by Burkholderia pseudomallei through the Virulence Factor TssM

Tan

Chen²,

Lim

et al. 2010

The Journal of Immunology

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Burkholderia pseudomallei is a Gram-negative saprophyte that is the causative agent of melioidosis, a severe infectious disease endemic in Northern Australia and Southeast Asia. This organism has sparked much scientific interest in the West because of its classification as a potential bioterrorism agent by the U.S. Centers for Disease Control and Prevention. However, relatively little is known about its pathogenesis. We demonstrate that B. pseudomallei actively inhibits NF-κB and type I IFN pathway activation, thereby downregulating host inflammatory responses. We found the virulence factor TssM to be responsible for this activity. TssM interferes with the ubiquitination of critical signaling intermediates, including TNFR-associated factor-3, TNFR-associated factor-6, and IκBα. The expression but not secretion of TssM is regulated by the type III secretion system. We demonstrate that TssM is important for B. pseudomallei infection in vivo as inflammation in the tssM mutant-infected mice is more severe and corresponds to a more rapid death compared with wild-type bacteria-infected mice. Abs to TssM can be detected in the sera of melioidosis patients, indicating that TssM is functionally expressed in vivo and thus could contribute to bacterial pathogenesis in human melioidosis.

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An Inv/Mxi‐Spa‐like type III protein secretion system in Burkholderia pseudomallei modulates intracellular behaviour of the pathogen

Cited by 253 publications

References 50 publications

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Differences in the Electrostatic Surfaces of the Type III Secretion Needle Proteins PrgI, BsaL, and MxiH

Suppression of Host Innate Immune Response by Burkholderia pseudomallei through the Virulence Factor TssM

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