Curli Fibers Are Required for Development of Biofilm Architecture in <i>Escherichia coli</i> K‐12 and Enhance Bacterial Adherence to Human Uroepithelial Cells

Kikuchi, Tatsuya; Mizunoe, Yoshimitsu; Takade, Akemi; Naito, Seiji; Yoshida, Shigeaki

doi:10.1111/j.1348-0421.2005.tb03678.x

Cited by 153 publications

(130 citation statements)

References 48 publications

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“…The glucosamine-6-phosphate isomerase NagB is part of the nag operon, whose genes are involved in the metabolism of N-acetylglucosamine 6-phosphate (GlcNAc6P), an important precursor of peptidoglycan and LPS synthesis. In E. coli, increases in the intracellular level of this precursor lead to the upregulation of the nag operon (Barnhart et al, 2006) and downregulation of curli and type 1 pili (Barnhart et al, 2006;Sohanpal et al, 2004), both known to be involved in biofilm formation (Kikuchi et al, 2005;Pratt & Kolter, 1998). Curli have been shown to assist in uroepithelial cell attachment in E. coli (Kikuchi et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

The high-affinity phosphate transporter Pst in Proteus mirabilis HI4320 and its importance in biofilm formation

et al. 2009

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Proteus mirabilis causes urinary tract infections (UTIs) in individuals requiring long-term indwelling catheterization. The pathogenesis of this uropathogen is mediated by a number of virulence factors and the formation of crystalline biofilms. In addition, micro-organisms have evolved complex systems for the acquisition of nutrients, including the phosphate-specific transport system, which has been shown to be important in biofilm formation and pathogenesis. A functional Pst system is important during UTIs caused by P. mirabilis HI4320, since transposon mutants in the PstS periplasmic binding protein and the PstA permease protein were attenuated in the CBA mouse model of UTI. These mutants displayed a defect in biofilm formation when grown in human urine. This study focuses on a comparison of the proteomes during biofilm and planktonic growth in phosphate-rich medium and human urine, and microscopic investigations of biofilms formed by the pst mutants. Our data suggest that (i) the Dpst mutants, and particularly the DpstS mutant, are defective in biofilm formation, and (ii) the proteomes of these mutants differ significantly from that of the wild-type. Therefore, since the Pst system of P. mirabilis HI4320 negatively regulates biofilm formation, this system is important for the pathogenesis of these organisms during complicated UTIs. INTRODUCTIONProteus mirabilis -a member of the family Enterobacteriaceae -is the most common aetiological agent responsible for complicated urinary tract infections (UTIs) (Mobley, 1996). Subpopulations at higher risk for infection by this pathogen include those with long-term indwelling catheterization as well as those with structural and functional abnormalities within the urinary tract (Mobley, 1996). Clinical syndromes associated with P. mirabilis include cystitis and pyelonephritis, with possible complications from stone formation and bacteraemia (Mobley, 1996). These micro-organisms survive in the urinary tract by virtue of their production of a battery of virulence factors, including urease, flagella, fimbriae, haemolysin and IgA protease (Belas, 1996;Mobley et al., 1994;Musher et al., 1975;Peerbooms et al., 1984; Walker et al., 1999), and formation of crystalline biofilm on indwelling catheters (Stickler et al., 1993).Biofilm formation -one of the most important mechanisms of pathogenicity of this micro-organism in the urinary tract -may be defined as a community of surface-attached bacteria encased in an extracellular matrix consisting of secreted carbohydrates, proteins and DNA. Indeed, biofilms have been associated with the virulence of a number of pathogens (Castelli et al., 2006). Organisms in these communities display phenotypic differences from planktonic cells, including a slower rate of growth and increased resistance to antibiotics (Lewis, 2001;Stoodley et al., 2002). P. mirabilis biofilms in urine are unique in that the extracellular polysaccharide matrix is enmeshed with struvite and carbonate apatite crystals (Jones et al., 2006).Abbreviations: CLSM, confocal ...

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Section: Discussionmentioning

confidence: 99%

The high-affinity phosphate transporter Pst in Proteus mirabilis HI4320 and its importance in biofilm formation

et al. 2009

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“…The biofilms of E. coli are partly composed of a functional amyloid nanofibre, curli, which plays a role in bacterial adhesion 44 , aggregation 43 and biofilm stability 37,45 . Our results show that the curli system in E. coli is capable of secreting a wide variety of chimeric CsgA-peptide constructs that can self-assemble into the ECM as amyloid nanofibres.…”

Section: Discussionmentioning

confidence: 99%

Programmable biofilm-based materials from engineered curli nanofibres

et al. 2014

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The significant role of biofilms in pathogenicity has spurred research into preventing their formation and promoting their disruption, resulting in overlooked opportunities to develop biofilms as a synthetic biological platform for self-assembling functional materials. Here we present Biofilm-Integrated Nanofiber Display (BIND) as a strategy for the molecular programming of the bacterial extracellular matrix material by genetically appending peptide domains to the amyloid protein CsgA, the dominant proteinaceous component in Escherichia coli biofilms. These engineered CsgA fusion proteins are successfully secreted and extracellularly self-assemble into amyloid nanofibre networks that retain the functions of the displayed peptide domains. We show the use of BIND to confer diverse artificial functions to the biofilm matrix, such as nanoparticle biotemplating, substrate adhesion, covalent immobilization of proteins or a combination thereof. BIND is a versatile nanobiotechnological platform for developing robust materials with programmable functions, demonstrating the potential of utilizing biofilms as large-scale designable biomaterials.

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“…Such structures facilitate binding to host tissues, interactions with other bacteria, secretion of molecules, and motility. Curli are produced by many members of the Enterobacteriaceae (6,56) and are associated with biofilm formation, host cell adhesion and invasion, and immune system activation (4,5,22,27,51,53,56). Curli fibers also share biochemical and structural characteristics with eukaryotic amyloid fibers and therefore provide an excellent model system for understanding amyloid fiber formation.…”

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confidence: 99%

GlcNAc-6P Levels Modulate the Expression of Curli Fibers byEscherichia coli

2006

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Curli are extracellular surface fibers that are produced by many members of the Enterobacteriaceae and contribute to biofilm formation. The environmental cues that promote biofilm formation are poorly understood. We found that deletion of the N-acetylglucosamine-6-phosphate (GlcNAc-6P) deacetylase gene, nagA, resulted in decreased transcription from the curli-specific promoters csgBA and csgDEFG and a corresponding decrease in curli production in Escherichia coli. nagA is in an operon that contains nagB, nagC, nagD, and nagE, whose products are required for utilization of GlcNAc as a carbon source. NagC is a repressor of the nagBACD and nagE genes in the absence of intracellular GlcNAc-6P. We found that nagC mutants were also defective in curli production. Growth of a wild-type strain on media containing additional GlcNAc reduced curli gene transcription to a level similar to the level observed when nagA was deleted. The defect in curli production in nagA or nagC mutants was alleviated by deletion of the GlcNAc transporter gene, nagE. Curli-producing ⌬nagA suppressor mutants whose cells were unable to take up GlcNAc were isolated. These results suggest that elevated levels of intracellular GlcNAc-6P signal cells to down-regulate curli gene expression.

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Curli Fibers Are Required for Development of Biofilm Architecture in Escherichia coli K‐12 and Enhance Bacterial Adherence to Human Uroepithelial Cells

Cited by 153 publications

References 48 publications

The high-affinity phosphate transporter Pst in Proteus mirabilis HI4320 and its importance in biofilm formation

The high-affinity phosphate transporter Pst in Proteus mirabilis HI4320 and its importance in biofilm formation

Programmable biofilm-based materials from engineered curli nanofibres

GlcNAc-6P Levels Modulate the Expression of Curli Fibers byEscherichia coli

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