Characterization of a respiratory mutant of Escherichia coli with reduced uptake of aminoglycoside antibiotics

Muir, Marianne E.; Hanwell, Dorothy R.; Wallace, Brian

doi:10.1016/0005-2728(81)90232-2

Cited by 27 publications

(16 citation statements)

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“…Aminoglycoside transport experiments determined that resistance is partially dependent upon proton-motive force (PMF). A decrease in the PMF potential results in a decrease in aminoglycoside uptake and an increase in resistance (62)(63)(64)(65). The identification of multiple ubi mutant strains in this study suggests that a fully functioning aerobic respiratory chain is necessary for DCS uptake and sensitivity.…”

Section: Discussionmentioning

confidence: 66%

“…K-12 ubiA and ubiD mutants were identified in the characterization of resistance to the antibiotics phleomycin and bleomycin (61). An E. coli K-12 ubiF mutant was isolated in a screen for resistance to the aminoglycoside streptomycin (62). This mutant strain displayed an increased resistance not only to streptomycin but also to other aminoglycosides, including gentamicin, kanamycin, and neomycin.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of Escherichia coli d -Cycloserine Transport and Resistant Mutants

2013

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b D-Cycloserine (DCS) is a broad-spectrum antibiotic that inhibits D-alanine ligase and alanine racemase activity. When Escherichia coli K-12 or CFT073 is grown in minimal glucose or glycerol medium, CycA transports DCS into the cell. E. coli K-12 cycA and CFT073 cycA mutant strains display increased DCS resistance when grown in minimal medium. However, the cycA mutants exhibit no change in DCS sensitivity compared to their parental strains when grown in LB (CFT073 and K-12) or human urine (CFT073 only). These data suggest that cycA does not participate in DCS sensitivity when strains are grown in a non-minimal medium. The small RNA GvcB acts as a negative regulator of E. coli K-12 cycA expression when grown in LB. Three E. coli K-12 gcvB mutant strains failed to demonstrate a change in DCS sensitivity when grown in LB. This further suggests a limited role for cycA in DCS sensitivity. To aid in the identification of E. coli genes involved in DCS sensitivity when grown on complex media, the Keio K-12 mutant collection was screened for DCS-resistant strains. dadA, pnp, ubiE, ubiF, ubiG, ubiH, and ubiX mutant strains showed elevated DCS resistance. The phenotypes associated with these mutants were used to further define three previously characterized E. coli DCS-resistant strains (316, 444, D -Cycloserine (DCS) is a broad-spectrum antibiotic produced by Streptomyces garyphalus, Streptomyces orchidaceus, andStreptomyces lavendulae. DCS is a cyclic, structural analog of D-alanine that inhibits alanine racemase and D-alanine ligase activity (1, 2). Inactivation of these enzymes results in a failure to produce mature peptidoglycan and an increased susceptibility to osmotic lysis. DCS is occasionally used as a second-line drug in the treatment of multidrug-resistant Mycobacterium tuberculosis infections (3, 4).DCS is not commonly used in chemotherapy regimens due to its adverse neurological side effects when administered at an effective dose (5). Unfortunately, physicians are increasingly being forced to use drugs like DCS to combat antibiotic-resistant bacterial infections. The development of new drugs is in high demand. The continued characterization of drugs like DCS could play a pivotal role in the development of novel drugs. The identification of additional DCS targets and the characterization of additional DCS resistance mechanisms could contribute to the development of new drugs with novel targets that possess less adverse effects.The Escherichia coli cycA gene codes for a permease that transports the antibiotic D-cycloserine and the amino acids ␤-/L-/Dalanine, glycine, and D-serine when grown in minimal glucose or glycerol media (6-10). A mutation in the cycA gene in the E. coli K-12 and the uropathogenic E. coli (UPEC) CFT073 strains results in increased DCS resistance when grown in a minimal medium (6,11,12). The resistance to and transport of DCS in a complex medium, like Luria Bertani (LB), or a biologically relevant medium, such as human urine, has not been reported for E. coli. As a result, the role cycA ...

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Section: Discussionmentioning

confidence: 66%

Section: Discussionmentioning

confidence: 99%

Characterization of Escherichia coli d -Cycloserine Transport and Resistant Mutants

2013

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“…A previously characterized ubiF mutant was found to show reduced uptake of gentamycin. At present, there is no evidence implicating Q in aminoglycoside antibiotic uptake and these observations are attributed to the general impairment of respiratory capacity (114). …”

Section: Q Biosynthesismentioning

confidence: 99%

Biosynthesis of Menaquinone (Vitamin K ₂ ) and Ubiquinone (Coenzyme Q)

Meganathan

Kwon

2009

EcoSal Plus

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Escherichia coli and Salmonella contain the naphthoquinones menaquinone (MK; vitamin K 2 ) and demethylmenaquinone and the benzoquinone ubiquinone (coenzyme Q; Q). Both quinones are derived from the shikimate pathway, which has been called a "metabolic tree with many branches." There are two different pathways for the biosynthesis of the naphthoquinones. The vast majority of prokaryotes, including E. coli and Salmonella , and the plants use the o -succinylbenzoate pathway, while a minority uses the futalosine pathway. The quinone nucleus of Q is derived directly from chorismate, while that of MK is derived from chorismate via isochorismate. The prenyl side chains of both quinones are from isopentenyl diphosphate formed by the 2- C -methyl-D-erythritol 4-phosphate (non-mevalonate) pathway and the methyl groups are from S -adenosylmethionine. In addition, MK biosynthesis requires 2-ketoglutarate and cofactors ATP, coenzyme A, and thiamine pyrophosphate. Despite the fact that both quinones originate from the shikimate pathway, there are important differences in their biosyntheses. The prenyl side chain in MK biosynthesis is introduced at the penultimate step, accompanied by decarboxylation, whereas in Q biosynthesis it is introduced at the second step, with retention of the carboxyl group. In MK biosynthesis, all the reactions of the pathway up to prenylation are carried out by soluble enzymes, whereas all the enzymes involved in Q biosynthesis except the first are membrane bound. In MK biosynthesis, the last step is a C -methylation; in Q biosynthesis, the last step is an O -methylation. In Q biosynthesis a second C -methylation and O -methylation take place in the middle part of the pathway. Despite the fact that Q and MK biosyntheses diverge at chorismate, the C -methylations in both pathways are carried out by the same methyltransferase.

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“…These observations can be explained by the dierence in the mechanisms of action of these antibiotics. Streptomycin is an antibiotic that directly interferes with respiration by inhibiting the synthesis of related protein (Baich and Couch, 1969;Muir et al, 1981Muir et al, , 1985Ojinsky et al, 1949), while ampicillin interferes with the synthesis of cellular membrane (Spratt, 1975;Suzuki et al, 1978;Tamaki et al, 1977). Because the microbial chip proposed here is based on the measurement of respiratory activity of E. coli, the assay system is especially sensitive to agents directly aecting cellular respiration, such as streptomycin.…”

Section: Resultsmentioning

confidence: 99%

“…While the respiratory image given in Figure 2a was stable for at least 5 h, the exposure to the solution of streptomycin changed the image drastically to that shown in Figure 2b. Streptomycin is an antibiotic known to inhibit an enzyme reaction that composes the respiratory chain (Baich and Couch, 1969;Muir et al, 1981Muir et al, , 1985Ojinsky et al, 1949), and thus acted to erase the respiratory image at the E. coli chip. It also would be worth noting that the treatment with streptomycin caused no signi®cant changes in the appearance of the E. coli spot.…”

Section: Methodsmentioning

confidence: 99%

A microbial chip combined with scanning electrochemical microscopy

Kaya

Nishizawa

Yasukawa

et al. 2001

Biotech & Bioengineering

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A microbial chip for bioassay was fabricated and its performance was characterized by scanning electrochemical microscopy (SECM). The microbial chip was prepared by spotting a suspension of Escherichia coli on a polystyrene substrate by using a glass capillary pen. The respiration activity of the E. coli spot was imaged with SECM by mapping the oxygen concentration around the spot. The SECM images of the microbial chips clearly showed spots with lower reduction currents, indicating that E. coli in the spots uptake oxygen by respiration. The bactericidal effects of antibiotics (streptomycin and ampicillin) were measured using the E. coli-based microbial chip, and discussed in comparison with the minimum inhibitory concentration (MIC) determined by an agar plate dilution method.

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Characterization of a respiratory mutant of Escherichia coli with reduced uptake of aminoglycoside antibiotics

Cited by 27 publications

References 28 publications

Characterization of Escherichia coli d -Cycloserine Transport and Resistant Mutants

Characterization of Escherichia coli d -Cycloserine Transport and Resistant Mutants

Biosynthesis of Menaquinone (Vitamin K ₂ ) and Ubiquinone (Coenzyme Q)

A microbial chip combined with scanning electrochemical microscopy

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Characterization of a respiratory mutant of Escherichia coli with reduced uptake of aminoglycoside antibiotics

Cited by 27 publications

References 28 publications

Characterization of Escherichia coli d -Cycloserine Transport and Resistant Mutants

Characterization of Escherichia coli d -Cycloserine Transport and Resistant Mutants

Biosynthesis of Menaquinone (Vitamin K 2 ) and Ubiquinone (Coenzyme Q)

A microbial chip combined with scanning electrochemical microscopy

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Biosynthesis of Menaquinone (Vitamin K ₂ ) and Ubiquinone (Coenzyme Q)