The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-1

Gibson, F.; Magrath, D. I.

doi:10.1016/0304-4165(69)90353-5

Cited by 310 publications

(176 citation statements)

References 23 publications

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“…The loss of virulence of the variants of the 0 18: K 1: H 7, Col V strain was caused by a decreased ability to invade the body. Williams (1979) andWarner et al (1981) showed that Col V carrying E. coli produced a Col V plasmid-determined siderophore, which was chemically a hydroxymate compound identical to aerobactin, originally described in 'Aerobacter aerogenes or Klebsiella' by Gibson & Magrath (1969). Similar findings were reported by Braun (1981).…”

Section: Haemolysinmentioning

confidence: 78%

Escherichia coliin extra-intestinal infections

Ørskov

1985

J. Hyg.

220

161

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When Theodor Escherich (1885a, b) first describedEscherichia colihe looked on it as a saprophytic organism. Soon several investigators found that colibacteria could be isolated from intestinal infections and from many infections outside the intestine, like urinary tract infections (UTI), cholecystitis, wound infections, meningitis, septicaemia, pulmonary infections, and many more. Uhlenhuth (1897) showed that coli strains from pathological processes were more pathogenic in animal experiments than strains isolated from the normal intestine. Smith (1927), who examined strains from white scours in calves, showed that spontaneous acapsular mutants could be obtained from certain colibacteria, and that such mutants were less virulent when injected intra-peritoneally into guinea-pigs.

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Section: Haemolysinmentioning

confidence: 78%

Escherichia coliin extra-intestinal infections

Ørskov

1985

J. Hyg.

220

161

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“…Aerobactin is a dihydroxamate siderophore derived by the condensation of a molecule of N6-acetyl N6-hydroxylysine to each of the two primary carboxyls of citric acid (10). This siderophore was originally discovered in Enterobacter aerogenes 62-I (formerly Aerobacter aerogenes) but is found in several members of the family Enterobacteriaceae (10,13,36).…”

mentioning

confidence: 99%

“…This siderophore was originally discovered in Enterobacter aerogenes 62-I (formerly Aerobacter aerogenes) but is found in several members of the family Enterobacteriaceae (10,13,36). Aerobactin is produced under conditions of iron deprivation, such as those found in body fluids and tissues of vertebrates (13).…”

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confidence: 99%

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Construction and biochemical characterization of recombinant cytoplasmic forms of the IucD protein (lysine:N6-hydroxylase) encoded by the pColV-K30 aerobactin gene cluster

et al. 1993

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The aerobactin gene cluster in pColV-K30 consists of five genes (iucABCD iutA); four of these (iucABCD) are involved in aerobactin biosynthesis, whereas the fifth one (iutA) encodes the ferriaerobactin outer membrane receptor. iucD encodes lysine:NM-hydroxylase, which catalyzes the first step in aerobactin biosynthesis. Regardless of the method used for cell rupture, we have consistently found that IucD remains membrane bound, and repeated efforts to achieve a purified and active soluble form of the enzyme have been unsuccessful. To circumvent this problem, we have constructed recombinant IucD proteins with modified amino termini by creating three in-frame gene fusions of IucD to the amino-terminal amino acids of the cytoplasmic enzyme 13-galactosidase. Two of these constructs resulted in the addition to the iucD coding region of a hydrophilic leader sequence of 13 and 30 amino acids. The other construct involved the deletion of the first 47 amino acids of the IucD amino terminus and the addition of 19 amino acids of the amino terminus of 1-galactosidase. Cells expressing any of the three recombinant IucD forms were found to produce soluble N6-hydroxylysine. One of these proteins, lucD439, was purified to homogeneity from the soluble fraction of the cell lysates, and it was capable of participating in the biosynthesis of aerobactin, as determined in vitro by a cell-free system and in vivo by a cross-feeding bioassay. A medium ionic strength of 0.25 (250 mM NaCl) or higher was required to maintain the protein in a catalytically functional, tetrameric state. The enzyme was stringently specific with regard to its substrate and cofactor, L-lysine and flavin adenine dinucleotide, respectively. NADPH appeared to be the preferred electron donor used by IucD439 in the N hydroxylation process.

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“…Aerobactin is a hydroxamate siderophore that is synthesized by strains of Aerobacter (now Enterobacter) aerogenes (for which it was named [11]), Enterobacter cloacae (28), Escherichia coli (3,13,30), and species of Klebsiella (16), Salmonella (8,21), and Shigella (20,23). In the case of E. coli, it is most frequently found among isolates from human urinary tract infections (5) and from septicemia of humans and domestic animals (5,22,27), and it has been proposed that the aerobactin iron uptake system can be considered to be a virulence determinant in such strains.…”

mentioning

confidence: 99%

RNA-DNA hybridization analysis of transcription of the plasmid ColV-K30 aerobactin gene cluster

Roberts¹,

Leavitt²,

Carbonetti³

et al. 1986

J Bacteriol

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Plasmid pABN1 contains the genetic determinants for the aerobactin iron uptake system of plasmid ColV-K30. Transposon Tn1000 mutants of pABN1 defective in synthesis of a 50,000-dalton polypeptide were found neither to secrete nor to accumulate aerobactin, but were not impaired in iron transport functions, clearly indicating a role for this polypeptide in aerobactin biosynthesis. RNA-DNA hybridization studies with probes spanning the entire aerobactin gene cluster showed that the system is regulated at the transcriptional level by the availability of iron in the external medium. When induced by low-iron stress, all five genes of the cluster were transcribed at a uniformly high level. When repressed by excess iron, transcripts of the four biosynthesis genes were some 30-fold less abundant in the case of the parental ColV-K30 plasmid and 10-fold less for the recombinant plasmid pABN1, whereas the receptor gene in either plasmid was transcribed at only about a third of the induced level.

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The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-1

Cited by 310 publications

References 23 publications

Escherichia coliin extra-intestinal infections

Escherichia coliin extra-intestinal infections

Construction and biochemical characterization of recombinant cytoplasmic forms of the IucD protein (lysine:N6-hydroxylase) encoded by the pColV-K30 aerobactin gene cluster

RNA-DNA hybridization analysis of transcription of the plasmid ColV-K30 aerobactin gene cluster

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