Transport of vitamin B12 in Escherichia coli: energy dependence

Bradbeer, Clive; Woodrow, M L

doi:10.1128/jb.128.1.99-104.1976

Cited by 48 publications

(19 citation statements)

References 24 publications

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“…Soo et al [99] showed that overexpression of YdaC increased overall fitness and resistance to erythromycin in E. coli. YdeO is a transcriptional regulator involved in E. coli acid resistance [100], and BtuB is an outermembrane transporter of vitamin B12, colicins and bacteriophages [101,102]. The accumulation of persistence-associated determinants, which included a porin, sulfatase, vitamin B12/ cobalamin outer-membrane transporter, transposase and hypothetical proteins, in a specific genomic region, suggests that these factors may be genetically linked.…”

Section: Discussionmentioning

confidence: 99%

Assessing the genomic relatedness and evolutionary rates of persistent verotoxigenic Escherichia coli serotypes within a closed beef herd in Canada

Wang

Jokinen²,

Laing

et al. 2020

Microbial Genomics

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Verotoxigenic Escherichia coli (VTEC) are food- and water-borne pathogens associated with both sporadic illness and outbreaks of enteric disease. While it is known that cattle are reservoirs of VTEC, little is known about the genomic variation of VTEC in cattle, and whether the variation in genomes reported for human outbreak strains is consistent with individual animal or group/herd sources of infection. A previous study of VTEC prevalence identified serotypes carried persistently by three consecutive cohorts of heifers within a closed herd of cattle. This present study aimed to: (i) determine whether the genomic relatedness of bovine isolates is similar to that reported for human strains associated with single source outbreaks, (ii) estimate the rates of genome change among dominant serotypes over time within a cattle herd, and (iii) identify genomic features of serotypes associated with persistence in cattle. Illumina MiSeq genome sequencing and genotyping based on allelic and single nucleotide variations were completed, while genome change over time was measured using Bayesian evolutionary analysis sampling trees. The accessory genome, including the non-protein-encoding intergenic regions (IGRs), virulence factors, antimicrobial-resistance genes and plasmid gene content of representative persistent and sporadic cattle strains were compared using Fisher’s exact test corrected for multiple comparisons. Herd strains from serotypes O6:H34 (n=22), O22:H8 (n=30), O108:H8 (n=39), O139:H19 (n=44) and O157:H7 (n=106) were readily distinguishable from epidemiologically unrelated strains of the same serotype using a similarity threshold of 10 or fewer allele differences between adjacent nodes. Temporal-cohort clustering within each serotype was supported by date randomization analysis. Substitutions per site per year were consistent with previously reported values for E. coli ; however, there was low branch support for these values. Acquisition of the phage-encoded Shiga toxin 2 gene in serotype O22:H8 was observed. Pan-genome analyses identified accessory regions that were more prevalent in persistent serotypes (P≤0.05) than in sporadic serotypes. These results suggest that VTEC serotypes from a specific cattle population are highly clonal with a similar level of relatedness as human single-source outbreak-associated strains, but changes in the genome occur gradually over time. Additionally, elements in the accessory genomes may provide a selective advantage for persistence of VTEC within cattle herds.

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Section: Discussionmentioning

confidence: 99%

Assessing the genomic relatedness and evolutionary rates of persistent verotoxigenic Escherichia coli serotypes within a closed beef herd in Canada

Wang

Jokinen²,

Laing

et al. 2020

Microbial Genomics

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“…Woodrow (18) found that the shock-sensitive transport of vitamin B12 in E. coli was driven by the energized state. Lieberman and Hong (1 9) have isolated a temperaturesensitive mutant in the common element of shock-sensitive and shock-resistant systems.…”

Section: Mamt:259mentioning

confidence: 99%

Energetics of galactose, proline, and glutamine transport in a cytochrome‐deficient mutant of salmonella typhimurium

Singh¹,

Bragg²

1977

J Supramol Struct

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The effect of inhibitors and uncouplers on the osmotic shock-sensitive transport systems for glutamine and galactose (by the beta-methyl galactoside permease) was compared to their effect on the osmotic shock-resistant proline and galactose permease systems in cytochrome-deficient cells of Salmonella typhimurium SASY28. Both osmotic shock-sensitive and -resistant systems were sensitive to uncouplers and to inhibitors of the membrane-bound Ca2+, Mg2+-activated adenosine triphosphatase. This suggests that uptake by both types of systems is energized in these cells by an electrochemical gradient of protons formed by ATP hydrolysis through the ATPase.

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“…In mammals, especially humans, several studies suggest that Cbl bound to transcobalamin-I1 (TC-11), one of the plasma carrier proteins, is bound to the cell surface receptor and internalized by pinocytosis (Seligman & Allen 1978 ;Youngdahl-Turner et al, 1979). In Escherichia coli Cbl uptake has been reported to be a biphasic process, consisting of Cbl binding to a cell surface receptor, which is a rapid initial phase, (Digirolamo & Bradbeer, 1971) and active transport coupled to metabolic energy, which is a slower secondary phase (Bradbeer & Woodrow, 1976). Some Cbl binding proteins have been purified from the cell envelope and from the periplasmic space of E. coli and have been well characterized (Kadner, 1978;Taylor et al, 1972).…”

Section: Introductionmentioning

confidence: 99%

Isolation of Pellicular Cobalamin-binding Proteins of the Cobalamin Uptake System of Euglena gracilis

et al. 1988

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Euglena gracilis pellicle, separated by sucrose density gradient centrifugation, had a high cobalamin (Cbl) binding activity, Of the Cbl binding protein 65% was solubilized from E. gracilis pellicle by using 0.1 % SDS/2 M-urea and the residual 35 % by using 1 % (w/v) SDS. Both of the Cbl binding protein fractions showed a broad pH dependence for the binding of Cbl. No evidence for the involvement of SH-groups or metal ions in Cbl binding was obtained. The K, values for cyanocobalamin of the proteins solubilized with 0.1 % SDS/2 M-urea and with 1 % SDS were 0.22 and 0.19 nM, respectively. The M , of a Cbl binding polypeptide of each protein was estimated to be 38000 by SDS-PAGE. The Cbl binding protein solubilized with 0.1 % SDS/2 Murea was purified to homogeneity. Inhibition experiments on Cbl uptake in E. gracilis cells, using an antibody against the Cbl binding protein solubilized with 0-1 % SDS/2 M-urea, showed that the Cbl binding proteins solubilized with 0.1 % SDS/2 M-urea and 1 % SDS take part in the slower secondary phase and in the initial rapid phase of Cbl uptake in E. gracilis, respectively.

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Transport of vitamin B12 in Escherichia coli: energy dependence

Cited by 48 publications

References 24 publications

Assessing the genomic relatedness and evolutionary rates of persistent verotoxigenic Escherichia coli serotypes within a closed beef herd in Canada

Assessing the genomic relatedness and evolutionary rates of persistent verotoxigenic Escherichia coli serotypes within a closed beef herd in Canada

Energetics of galactose, proline, and glutamine transport in a cytochrome‐deficient mutant of salmonella typhimurium

Isolation of Pellicular Cobalamin-binding Proteins of the Cobalamin Uptake System of Euglena gracilis

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