Thin, aggregative fimbriae mediate binding of Salmonella enteritidis to fibronectin

Collinson, S. Karen; Doig, P.; Doran, James L.; Clouthier, Sharon C.; Trust, Trevor J.; Kay, William W.

doi:10.1128/jb.175.1.12-18.1993

Cited by 185 publications

(181 citation statements)

References 38 publications

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“…This medium has been used to detect cell surface appendages, extracellular matrix production, A- layer proteins, and as an indicator of virulence (Kay et al, 1985;Collinson et al, 1993;Romling and Rohde, 1999;Romling et al, 2000;Zogaj et al, 2003;Friedman and Kolter, 2004). OP or TR parental strains have rough colony morphologies when grown on Congo red medium (Fig.…”

Section: Pellicles With Subtle Defects Have Lesions Causing Altered Cmentioning

confidence: 99%

Genetic determinants of biofilm development of opaque and translucent Vibrio parahaemolyticus

Enos-Berlage

Güvener

Keenan

et al. 2005

Molecular Microbiology

207

193

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SummaryVibrio parahaemolyticus isolates display variation in colony morphology, alternating between opaque (OP) and translucent (TR) cell types. Phase variation is the consequence of genetic alterations in the locus encoding the quorum sensing output regulator OpaR. Here, we show that both cell types form stable, but distinguishable biofilms that differ with respect to attachment and detachment profiles to polystyrene, pellicle formation and stability at the air/medium interface, and submerged biofilm architecture and dispersion at a solid/liquid interface. The pellicle, which is a cohesive mat of cells, was exploited to identify mutants having altered or defective biofilm formation. Transposon insertion mutants were obtained with defects in genes affecting multiple cell surface characteristics, including extracellular polysaccharide, mannose-sensitive haemagglutinin type 4 pili and polar (but not lateral) flagella. Other insertions disrupted genes coding for potential secreted proteins or transporters of secreted proteins, specifically haemolysin co-regulated protein and an RTX toxin-like membrane fusion transporter, as well as potential modifiers of cell surface molecules ( nagAC operon). The pellicle screen also identified mutants with lesions in regulatory genes encoding H-NS, a CsgD-like repressor and an AraC-like protein. This work initiates the characterization of V. parahaemolyticus biofilm formation in the OP and TR cell types and identifies a diverse repertoire of cell surface elements that participate in determining multicellular architecture.

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Section: Pellicles With Subtle Defects Have Lesions Causing Altered Cmentioning

confidence: 99%

Genetic determinants of biofilm development of opaque and translucent Vibrio parahaemolyticus

Enos-Berlage

Güvener

Keenan

et al. 2005

Molecular Microbiology

207

193

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“…s 38 is involved in the gene regulatory network governing the rdar phenotype; in early stationary phase, it activates the transcription of a key regulator in rdar formation, agfD. AgfD (CsgD) is a transcriptional regulator that initiates transcription in the agfBAC operon, which encodes the main structural proteins for fimbrial biosynthesis (Collinson et al, 1993(Collinson et al, , 1996Rö mling et al, 1998Rö mling et al, , 2000. agfD is also regulated by the transcriptional regulators OmpR, MlrA and CpxR-P (Gerstel and Rö mling, 2003;.…”

Section: Introductionmentioning

confidence: 99%

“…Rdar formation is the result of coordinated expression of genes required for biosynthesis of fimbriae (Collinson et al, 1993(Collinson et al, , 1996Rö mling andRohde, 1999, 2000), cellulose (Rö mling et al, 2000;Zogaj et al, 2001) and additional polysaccharides . s 38 is involved in the gene regulatory network governing the rdar phenotype; in early stationary phase, it activates the transcription of a key regulator in rdar formation, agfD.…”

Section: Introductionmentioning

confidence: 99%

Evolutionary loss of the rdar morphotype in Salmonella as a result of high mutation rates during laboratory passage

2008

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Rapid evolution of microbes under laboratory conditions can lead to domestication of environmental or clinical strains. In this work, we show that domestication due to laboratory passage in rich medium is extremely rapid. Passaging of wild-type Salmonella in rich medium led to diversification of genotypes contributing to the loss of a spatial phenotype, called the rdar morphotype, within days. Gene expression analysis of the rdar regulatory network demonstrated that mutations were primarily within rpoS, indicating that the selection pressure for scavenging during stationary phase had the secondary effect of impairing this highly conserved phenotype. If stationary phase was omitted from the experiment, radiation of genotypes and loss of the rdar morphotype was also demonstrated, but due to mutations within the cellulose biosynthesis pathway and also in an unknown upstream regulator. Thus regardless of the selection pressure, rapid regulatory changes can be observed on laboratory timescales. The speed of accumulation of rpoS mutations during daily passaging could not be explained by measured fitness and mutation rates. A model of mutation accumulation suggests that to generate the observed accumulation of r 38 mutations, this locus must experience a mutation rate of approximately 10 À4 mutations/gene/generation. Sequencing and gene expression of population isolates indicated that there were a wide variety of r 38 phenotypes within each population. This suggests that the rpoS locus is highly mutable by an unknown pathway, and that these mutations accumulate rapidly under common laboratory conditions.

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“…Because of the amyloid properties of curli fibers (5,6), the colonies of curli-producing Escherichia coli stain red when grown on Congo red indicator plates, which provides a convenient assay to monitor curli assembly in vivo (7). In E. coli, at least six proteins are dedicated to directing efficient curli formation.…”

mentioning

confidence: 99%

Gatekeeper residues in the major curlin subunit modulate bacterial amyloid fiber biogenesis

Wang

Zhou

Ren

et al. 2009

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

117

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Amyloid fibers are filamentous protein structures commonly associated with neurodegenerative diseases. Unlike disease-associated amyloids, which are the products of protein misfolding, Escherichia coli assemble membrane-anchored functional amyloid fibers called curli. Curli fibers are composed of two proteins, CsgA and CsgB. In vivo, the polymerization of the major curli subunit protein, CsgA, is dependent on CsgB-mediated nucleation. The amyloid core of CsgA features five imperfect repeats (R1-R5), and R1 and R5 govern CsgA responsiveness to CsgB nucleation and self-seeding by CsgA fibers. Here, the specificity of bacterial amyloid nucleation was probed, revealing that certain aspartic acid and glycine residues inhibit the intrinsic aggregation propensities and nucleation responsiveness of R2, R3, and R4. These residues function as "gatekeepers" to modulate CsgA polymerization efficiency and potential toxicity. A CsgA molecule lacking gatekeeper residues polymerized in vitro significantly faster than wild-type CsgA and polymerized in vivo in the absence of the nucleation machinery, resulting in mislocalized fibers. This uncontrolled polymerization was associated with cytotoxicity, suggesting that incorrectly regulated CsgA polymerization was detrimental to the cell.A myloids are ordered proteinaceous fibers commonly associated with mammalian neurodegenerative diseases and prion-based encephalopathies (1). Amyloid fibers have distinct biochemical and biophysical properties, such as remarkable resistance to chemical and thermal denaturation, and specific tinctorial properties when bound to Congo red and thioflavin T (ThT) (1). The molecular basis of neurodegenerative disease development induced by amyloid propagation remains elusive, partially because of the seemingly erratic and uncontrolled nature of amyloidogenesis. An emerging focus of amyloid biosynthesis has shown that amyloids can also be an integral part of physiology found in different organisms including bacteria, fungi, and mammals (2, 3). How nature coordinates functional amyloid propagation and reduces the associated cytotoxicity is poorly understood.Curli, a bacterially produced functional amyloid, is an important component of the extracellular matrix and is involved in bacterial community behaviors (4). Because of the amyloid properties of curli fibers (5, 6), the colonies of curli-producing Escherichia coli stain red when grown on Congo red indicator plates, which provides a convenient assay to monitor curli assembly in vivo (7). In E. coli, at least six proteins are dedicated to directing efficient curli formation. Curli fibers are composed of a major subunit CsgA and a minor subunit CsgB. CsgA remains unpolymerized until it encounters the surface-tethered nucleator CsgB, which initiates CsgA polymerization (8). CsgD is a transcriptional activator for the csgBA operon (4). CsgG, CsgE, and CsgF are nonfiber structural accessory proteins involved in secretion and stabilization of the fiber subunits and modulation of fiber assembly (6). CsgG is prop...

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Thin, aggregative fimbriae mediate binding of Salmonella enteritidis to fibronectin

Cited by 185 publications

References 38 publications

Genetic determinants of biofilm development of opaque and translucent Vibrio parahaemolyticus

Genetic determinants of biofilm development of opaque and translucent Vibrio parahaemolyticus

Evolutionary loss of the rdar morphotype in Salmonella as a result of high mutation rates during laboratory passage

Gatekeeper residues in the major curlin subunit modulate bacterial amyloid fiber biogenesis

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