Construction and expression of recombinant plasmids encoding type 1 or D-mannose-resistant pili from a urinary tract infection Escherichia coli isolate

Hull, Richard A.; Gill, Richard; Hsu, Pei-Yung; Minshew, Barbara H.; Falkow, Stanley

doi:10.1128/iai.33.3.933-938.1981

Cited by 557 publications

(215 citation statements)

References 21 publications

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“…P pili show the strongest association with severe UTI in epidemiological studies (Bergsten et al, 2005). They are encoded by the pap (pyelonephritis-associated pili) gene cluster (Hull et al, 1981;Vaisanen et al, 1981). P pili are c. 7 nm wide and consist of PapA subunits.…”

Section: Colonization Of the Urinary Tractmentioning

confidence: 99%

Physical stress and bacterial colonization

Otto¹

2014

FEMS Microbiol Rev

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Bacterial surface colonizers are subject to a variety of physical stresses. During the colonization of human epithelia such as on the skin or the intestinal mucosa, bacteria mainly have to withstand the mechanical stress of being removed by fluid flow, scraping, or epithelial turnover. To that end, they express a series of molecules to establish firm attachment to the epithelial surface, such as fibrillar protrusions (pili) and surface-anchored proteins that bind to human matrix proteins. In addition, some bacteria – in particular gut and urinary tract pathogens – use internalization by epithelial cells and other methods such as directed inhibition of epithelial turnover to ascertain continued association with the epithelial layer. Furthermore, many bacteria produce multi-layered agglomerations called biofilms with a sticky extracellular matrix, providing additional protection from removal. This review will give an overview over the mechanisms human bacterial colonizers have to withstand physical stresses with a focus on bacterial adhesion.

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Section: Colonization Of the Urinary Tractmentioning

confidence: 99%

Physical stress and bacterial colonization

Otto¹

2014

FEMS Microbiol Rev

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“…Cells from 1 ml of overnight broth cultures were obtained by centrifugation (12000 Xg, 2 min, room temperature) and resuspended in 75 yl of 0.25 M sucrose in 50 mM Tris-HCl buffer, pH 8.0 (lysis buffer) and lysed by successive incubations with mutanolysin (45 pg) and SDS (1% final concentration) [20]. DNA was extracted by ethanol precipitation following the salting-out of proteins.…”

Section: Preparation Of Chromosomal Dnamentioning

confidence: 99%

The prevalence of gentamicin 2′-N-acetyltransferase in the Proteeae and its role in the O-acetylation of peptidoglycan

Clarke¹

1996

FEMS Microbiology Letters

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The prevalence of aac(2')-Ia, a gene coding for gentamicin 2'-N-acetyltransferase in Providencia stuartii, among species of the Proteeae was investigated to determine if it is a common resistance factor and whether the correlation observed in P. stuartii between its expression and the levels of peptidoglycan O-acetylation represents a general feature of bacteria producing this form of modified peptidoglycan. An evaluation of the MICs of gentamicin for each of the species of the Proteeae did not reveal any apparent relationship between resistance and the degree of O-acetylation of peptidoglycan. The entire aac(2')-Ia gene was used as a probe in Southern hybridization experiments against genomic DNA from each species of the Proteeae. A sequence with strong homology to aac(2')-Ia was present only in Proteus penneri while weak hybridization was also observed to the restriction digested DNA from Providencia rettgeri. Other bacteria that O-acetylate peptidoglycan were also screened with this probe and a homologous DNA sequence was only found in Neisseria subflava. These data suggest that AAC(2')-Ia may contribute to the O-acetylation of peptidoglycan in P. stuartii, but a more specific enzyme must also be produced for this function.

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“…The phenylthiohydantoin amino acids were identified using a Beckman HPLC gradient system with an IBM 5 (xm cyano column. The solvent systems and elution procedures were essentially as described by Hunkapillar and Hood (1983).…”

Section: Amino Acid Analysesmentioning

confidence: 99%

Cloning and nucleotide sequence analysis of the serotype 2 fimbrial subunit gene of Bordetella pertussis

Livey

Duggleby

Robinson

1987

Molecular Microbiology

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An oligonucleotide probe complementary to the beginning of the gene encoding the serotype 2(ST2) fimbrial subunit of Bordetella pertussis was synthesized and a cloned DNA fragment hybridizing with the probe identified and sequenced. Several lines of evidence indicate that an open reading frame with coding information for a polypeptide of 207 amino acids, including a 26-amino-acid signal sequence, is the ST2 gene. The protein deduced from the nucleotide sequence shows good agreement with the NH2-terminal amino acid sequence, amino acid composition and molecular weight of the purified fimbrial subunit. In addition, the proposed ST2 subunit is shown to have homology with other fimbrial subunits.

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Construction and expression of recombinant plasmids encoding type 1 or D-mannose-resistant pili from a urinary tract infection Escherichia coli isolate

Cited by 557 publications

References 21 publications

Physical stress and bacterial colonization

Physical stress and bacterial colonization

The prevalence of gentamicin 2′-N-acetyltransferase in the Proteeae and its role in the O-acetylation of peptidoglycan

Cloning and nucleotide sequence analysis of the serotype 2 fimbrial subunit gene of Bordetella pertussis

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