Differential regulation of fasA and fasH expression of Escherichia coli 987P fimbriae by environmental cues

Edwards, Robert A.; Schifferli, Dieter M.

doi:10.1046/j.1365-2958.1997.5161875.x

Cited by 47 publications

(66 citation statements)

References 48 publications

(68 reference statements)

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“…Many other fimbrial systems use AraClike transcriptional activators to regulate gene expression and often the regulator is immediately adjacent to the fimbrial operon, as is found for the sef operon. For example, the 987P fimbria in enterotoxigenic E. coli utilizes a homologous regulator (FasH) to activate gene transcription (Edwards & Schifferli, 1997). The similarity and location of these regulators and the similar organization of the fimbrial operons as a whole [in general they are organized major subunit-chaperoneusher-(optional minor subunits)-regulator] suggests that many fimbrial operons have evolved from some common ancestor.…”

Section: Discussionmentioning

confidence: 99%

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Genomic analysis and growth-phase-dependent regulation of the SEF14 fimbriae of Salmonella enterica serovar Enteritidis The GenBank accession number for the sequence reported in this paper is AF239978.

et al. 2001

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Salmonella enterica serovar Enteritidis is a leading cause of food poisoning in the USA and Europe. Although Salmonella serovars share many fimbrial operons, a few fimbriae are limited to specific Samonella serovars. SEF14 fimbriae are restricted to group D Salmonella and the genes encoding this virulence factor were acquired relatively recently. Genomic, genetic and gene expression studies have been integrated to investigate the ancestry, regulation and expression of the sef genes. Genomic comparisons of the Salmonella serovars sequenced revealed that the sef operon is inserted in leuX in Salmonella Enteritidis, Salmonella Paratyphi and Salmonella Typhi, and revealed the presence of a previously unidentified 25 kb pathogenicity island in Salmonella Typhimurium at this location. Salmonella Enteritidis contains a region of homology between the Salmonella virulence plasmid and the chromosome downstream of the sef operon. The sef operon itself consists of four co-transcribed genes, sefABCD, and adjacent to sefD there is an AraC-like transcriptional activator that is required for expression of the sef genes. Expression of the sef genes was optimal during growth in late exponential phase and was repressed during stationary phase. The regulation was coordinated by the RpoS sigma factor.

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Section: Discussionmentioning

confidence: 99%

“…Salmonella Enteritidis contains a potent restriction system that limits genetic manipulations in this strain. (Caron et al, 1989 ;Edwards & Schifferli, 1997 ;Jost & Adler, 1993 ;Nataro et al, 1994 ;Tobe et al, 1996).…”

Section: Transduction Of the Sef Island To Salmonella Typhimurium Lt2mentioning

confidence: 99%

Genomic analysis and growth-phase-dependent regulation of the SEF14 fimbriae of Salmonella enterica serovar Enteritidis The GenBank accession number for the sequence reported in this paper is AF239978.

et al. 2001

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“…An intriguing hypothesis is that intestinal glucose concentrations may actually influence which regions of the small intestine are most efficiently colonized by different bacterial pathogens (Edwards and Schifferli, 1997). For example, the expression of certain pili in enterotoxinogenic E. coli strains is negatively regulated by glucose (Isaacson, 1980;Edwards and Schifferli, 1997), and these bacteria efficiently colonize the distal regions of the small intestine where glucose levels are lower than in the more proximal regions (Moon et al, 1979;Ferraris et al, 1990). Such findings raise the possibility that intraintestinal glucose concentrations contribute to the ability of V. cholerae to colonize the proximal regions of the small intestine.…”

Section: Influence Of Camp-crp On the Environmental Control Of The Tomentioning

confidence: 99%

Control of the ToxR virulence regulon in Vibrio cholerae by environmental stimuli

Skorupski

Taylor

1997

Molecular Microbiology

224

187

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SummaryMany bacterial pathogens regulate the expression of virulence genes in a co-ordinate manner in response to changes in the environment. For example, the human pathogen, Vibrio cholerae, possesses a virulence regulon composed of over 20 genes involved in colonization, toxin production and bacterial survival within the host, which are co-ordinately regulated by external stimuli, such as temperature, pH and osmolarity. Although the expression of the regulon is dependent upon the transcriptional activator ToxR, most of these genes are controlled by a second transcriptional activator, ToxT, which is itself positively regulated by ToxR. The mechanisms by which environmental stimuli influence the ToxR regulon are not yet understood, but ToxR-mediated control over the expression of toxT clearly plays a role. The recent finding that the global regulator cAMP-CRP also influences the expression of the ToxR regulon under various environmental conditions raises new issues regarding the pathways and mechanisms by which this regulation is achieved and indicates that multiple overlapping systems are involved.

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“…Media and Reagents-Wild-type E. coli strain 987 was grown in minimal medium E supplemented with pantothenic acid and glycerol (35). Strain JM109 was used for recombinant DNA work.…”

Section: Bacterial Strains and Plasmidmentioning

confidence: 99%

“…Strain JM109 was used for recombinant DNA work. Strain B834(DE3) (Novagen, Madison, WI) was used for 35 S-labeling of the 987P fimbriae. Strain BL21(DE3) was used for the expression of a porcine histone H1 protein and partial fragments of it.…”

Section: Bacterial Strains and Plasmidmentioning

confidence: 99%

Histone H1 Proteins Act As Receptors for the 987P Fimbriae of Enterotoxigenic Escherichia coli

Zhu¹,

Chen

Choi³

et al. 2005

Journal of Biological Chemistry

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The tip adhesin FasG of the 987P fimbriae of enterotoxigenic Escherichia coli mediates two distinct adhesive interactions with brush border molecules of the intestinal epithelial cells of neonatal piglets. First, FasG attaches strongly to sulfatide with hydroxylated fatty acyl chains. This interaction involves lysine 117 and other lysine residues of FasG. Second, FasG recognizes specific intestinal brush border proteins that migrate on a sodium-dodecyl sulfate-polyacrylamide gel like a distinct set of 32-35-kDa proteins, as shown by ligand blotting assays. The protein sequence of high performance liquid chromatography-purified tryptic fragments of the major protein band matched sequences of human and murine histone H1 proteins. Porcine histone H1 proteins isolated from piglet intestinal epithelial cells demonstrated the same SDS-PAGE migration pattern and 987P binding properties as the 987P-specific protein receptors from porcine intestinal brush borders. Binding was dose-dependent and shown to be specific in adhesion inhibition and gel migration shift assays. Moreover, mapping of the histone H1 binding domain suggested that it is located in their lysine-rich C-terminal domains. Histone H1 molecules were visualized on the microvilli of intestinal epithelial cells by immunohistochemistry and electron microscopy. Taken together these results indicated that the intestinal protein receptors for 987P are histone H1 proteins. It is suggested that histones are released into the intestinal lumen by the high turnover of the intestinal epithelium. Their strong cationic properties can explain their association with the negatively charged brush border surfaces. There, the histone H1 molecules stabilize the sulfatide-fimbriae interaction by simultaneously binding to the membrane and to 987P. Enterotoxigenic Escherichia coli (ETEC)1 cause diarrhea in mammals by expressing at least one type of enteroadhesive fimbria and one type of enterotoxin. By adhering to intestinal epithelial cells, localized multiplication of an ETEC strain can progress to mucosal surface colonization and concomitant effective enterotoxin delivery. This was illustrated with hostspecific ETEC strains in both animals and human volunteers (1-5). ETEC are the most important etiologic agents of both neonatal and postweaning diarrhea in pigs (6, 7). 987P-fimbriated ETEC cause diarrhea in neonatal piglets in the United States (8), Europe (9, 10), Asia (11-15), and Central and South America (16 -18). In addition to this widespread distribution, the recent identification of human ETEC strains with 987P-like fimbriae (19, 20) on various continents highlights the evolutionary adaptability of these fimbriae (21).The 987P fimbria consists of the helical arrangement of protein subunits along a filamentous axis (22,23). It is a heteropolymeric structure that is made up of one major subunit, FasA, and two minor subunits, FasF and FasG (24). Fimbriae are not produced in the absence of any of these subunits (25). Electron microscopy and export studies indicated that FasG ...

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Differential regulation of fasA and fasH expression of Escherichia coli 987P fimbriae by environmental cues

Cited by 47 publications

References 48 publications

Genomic analysis and growth-phase-dependent regulation of the SEF14 fimbriae of Salmonella enterica serovar Enteritidis The GenBank accession number for the sequence reported in this paper is AF239978.

Genomic analysis and growth-phase-dependent regulation of the SEF14 fimbriae of Salmonella enterica serovar Enteritidis The GenBank accession number for the sequence reported in this paper is AF239978.

Control of the ToxR virulence regulon in Vibrio cholerae by environmental stimuli

Histone H1 Proteins Act As Receptors for the 987P Fimbriae of Enterotoxigenic Escherichia coli

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