Porin-mediated cephalosporin resistance in <i>Escherichia coli</i> K-12

Curtis, Nigel A. C.; Eisenstadt, Rosemary L.; Turner, Kath A.; White, Anthony J.

doi:10.1093/jac/15.5.642

Cited by 21 publications

(10 citation statements)

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“…(Tables 2 and 3). This was in contrast to results for E. coli and other members of the family Enterobacteriaceae in which porin-deficient mutants were 8-to 32-fold more resistant to certain antibiotics (4,7,17,20,23 (Table 3). This dichotomy in levels of increase in resistance to P-lactam antibiotics of porin-deficient E. coli strains (i.e., large versus small increases) has been previously noted by other researchers (7,17).…”

Section: Methodscontrasting

confidence: 86%

“…Recently, the gene for protein F was sequenced (7). Sequence homology between protein F and other outer membrane proteins was not extensive.…”

Section: Methodsmentioning

confidence: 99%

“…This proposal is based largely on observations, in strains of the family Enterobacteriaceae, showing that cells lacking porin proteins in their outer membranes were more resistant than wild-type strains to hydrophilic antibiotics, particularly P-lactams (7,17,18,20,23). However, for some of the more recently introduced P-lactams, there is still some dispute, based on similar studies, as to the role of Escherichia coli porins in their uptake across the outer membrane (7,17).. In many instances, however, model membrane studies have supported a role for porins in antibiotic uptake (14,29,38).…”

mentioning

confidence: 99%

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Construction and characterization of Pseudomonas aeruginosa protein F-deficient mutants after in vitro and in vivo insertion mutagenesis of the cloned gene

Woodruff

Hancock

1988

J Bacteriol

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Mutants with insertion mutations in the Pseudomonas aeruginosa protein F (oprF) gene were created in vivo by Tn1 mutagenesis of the cloned gene in Escherichia coli and in vitro by insertion of the streptomycin resistance-encoding omega fragment into the cloned gene, followed by transfer of the mutated protein F gene back to P. aeruginosa. Homologous recombination into the P. aeruginosa chromosome was driven by a bacteriophage F116L transduction method in the oprF::Tn1 mutants or Tn5-instability in the oprF::omega mutants. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western immunoblotting demonstrated that the resultant oprF insertion mutants had lost protein F, whereas restriction digestion and Southern blotting experiments proved that the mutants contained a single chromosomal oprF gene with either Tn1 or omega inserted into it. It has been proposed that protein F has a role in antibiotic uptake in P. aeruginosa. Measurement of antibiotic resistance levels showed small to marginal increases in resistance, compared with that of the parent P. aeruginosa strain, to a variety of beta-lactam antibiotics. Protein F-deficient mutants had altered barrier properties as revealed by a three- to fivefold increase in the uptake of the hydrophobic fluorescent probe 1-N-phenylnaphthylamine.

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Section: Methodscontrasting

confidence: 86%

“…Recently, the gene for protein F was sequenced (7). Sequence homology between protein F and other outer membrane proteins was not extensive.…”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Construction and characterization of Pseudomonas aeruginosa protein F-deficient mutants after in vitro and in vivo insertion mutagenesis of the cloned gene

Woodruff

Hancock

1988

J Bacteriol

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“…The primary target site for these compounds is PBP 3, in common with other cephalosporins of this class (3), and the morphological response to growth at concentrations close to the MIC (namely, filamentation) would agree with this PBP being the major target. It was interesting to note that, in the case of Ro 19-5247, there was an eightfold (or greater) difference between the prime PBP target I50 and the MIC.…”

Section: Resultsmentioning

confidence: 93%

“…In common with other aminothiazoly cephalosporins, alterations in the expression of porin proteins in the outer membrane of the bacterial cell (ompR and envZ) do not cause a decrease in susceptibility to these two compounds as seen with other early cephalosporins (3,4).…”

Section: Resultsmentioning

confidence: 93%

In vitro activity of Ro 15-8074 and Ro 19-5247, two orally administered cephalosporin metabolites

Wise¹,

Andrews²,

Piddock³

1986

Antimicrob Agents Chemother

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The activity of two iminomethoxy aminothiazoly cephalosporins, Ro 15-8074 and Ro 19-5247, was compared with that of other P-lactams against a total of 491 bacterial strains. Both were highly active (MIC for 90% of the strains tested [MIC90], s2 pug/mi) against the majority of the members of the family Enterobacteriaceae, Haemophilus influenzae, Neisseria spp., and Streptococcus pneumoniae, being at least 16-fold more active than cephalexin and 8-fold more active than cefuroxime. There was no activity against Pseudomonas aeruginosa and poor activity against Morganella morganii (in the case of Ro 15-8074), Enterobacter sp., and Citrobacter sp.

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The Ferric Hydroxamate Uptake ReceptorFhuAand RelatedTonB‐Dependent Transporters in the Outer Membrane of Gram‐Negative Bacteria

Ferguson

Coulton

Diederichs

et al. 2004

Handbook of Metalloproteins

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FUNCTIONAL CLASS chemiosmotic gradient; ABC transporter; bacteriophage infection; colicin import; siderophore-antibiotic conjugate and peptide antibiotic sensitivity; Ton B-dependent receptor; structurally related to the ferric enterobactin receptor, and Active transporter; siderophore; integral outer membrane protein; ferric hydroxamate uptake receptor, known as FhuA; (a) (b) 3D Structure The three-dimensional structure of FhuA in complex with ferricrocin. (a) FhuA in ribbon representation. The view is perpendicular to the barrel axis. The strands that comprise the front of th e barrel domain have bee n removed to provide an un obstructed view of the cork domain. (b) FlllI A as viewed from th e externa l environment along the barrel axis. In panels a and b, the bar rel domalll (residues 161-714) and the cork domain (residues 1-160) are colored blue and ye ll ow, respectively. The ferr icrocin molecule IS shown as a bond model with carbon atoms white, oxygen atoms red, and nitrogen atoms blue. The ::rric iron atom is shown as a large red sphere. These and all the following color fi gures were prepared using MOLSCl111'T 95 ancl I1AST EII3 D. PDB code: IQFF. 834 FClnclu'O llle T I. 1'5.<1'80. UC-I Col /vl M 1C1OC li t J25 Dbs !\ lboIllYCIll Rhodotul1I lil le Elll erob.1clill Dill> Dbh CGP ,ISJ, Aeroonelill ('o!>l oge n Col B.D Col ln.lb.V ('01 G,II

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Porin-mediated cephalosporin resistance in Escherichia coli K-12

Cited by 21 publications

References 0 publications

Construction and characterization of Pseudomonas aeruginosa protein F-deficient mutants after in vitro and in vivo insertion mutagenesis of the cloned gene

Construction and characterization of Pseudomonas aeruginosa protein F-deficient mutants after in vitro and in vivo insertion mutagenesis of the cloned gene

In vitro activity of Ro 15-8074 and Ro 19-5247, two orally administered cephalosporin metabolites

The Ferric Hydroxamate Uptake ReceptorFhuAand RelatedTonB‐Dependent Transporters in the Outer Membrane of Gram‐Negative Bacteria

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