Hydroxamate-mediated transport of iron controlled by ColV plasmids

Stuart, S J; Greenwood, Kenneth T.; Luke, R. K. J.

doi:10.1128/jb.143.1.35-42.1980

Cited by 74 publications

(43 citation statements)

References 33 publications

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“…Both species of Neisseria gave a positive reaction for bound hydroxylamine, indicative of production of hydroxamate siderophores by these microorganisms. Again, the quantity of material produced by the meningococcus was greater than that produced by the gonococcus, although the amount produced by both organisms was considerably lower than that produced by other microorganisms (6,10,26), and it could not be detected in unconcentrated culture supernatant fluids.…”

Section: Resultsmentioning

confidence: 79%

Siderophore Production by Pathogenic Neisseria spp

Yancey

Finkelstein

1981

Infect Immun

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Previous studies have established the importance of iron acquisition to the growth and virulence of Neisseria meningitidis and Neisseria gonorrhoeae. Although preliminary evidence that the Neisseria spp. produce siderophores has been presented, the exact mechanism of iron acquisition has remained obscure. Siderophore production by N. gonorrhoeae and N. meningitidis was induced in two different low-iron media. The iron-reactive siderophores, "gonobactin" and "meningobactin," were partially purified by ion exchange chromatography followed by extraction with phenol-chloroform-ether or by gel filtration. The compounds were of low molecular weight, their synthesis was repressed by iron in the medium, and they appeared to be hydroxamic acids since they were stimulatory for Arthrobacter flavescens JG-9 (a hydroxamate auxotroph) and gave a positive Csaky reaction for bound hydroxylamine. In the iron form, the compounds had an absorption maximum of approximately 420 nm. Although meningobactin stimulated growth of the gonococcus in low-iron media and vice versa, the homologous activity was more marked, indicating that the compounds, though similar, were probably not identical. As determined by A. flavescens assay the meningococcus produced three to five times more siderophore than did the gonococcus; however, the amount of siderophore present in the culture fluids of even the meningococcus was 100to 1,000-fold lower than the concentration of hydroxamate siderophores reported to be produced by Bacillus megaterium or Aerobacter aerogenes. Virulent, colony type 1 N. gonorrhoeae produced significantly more gonobactin than did the avirulent colony type 3 gonococci. MATERIALS AND METHODSBacterial strains. Neisseria strains were as previously described (22,28). Bacillus megaterium ATCC 19213 and Arthrobacter flavescens JG-9 were obtained from C. E. Lankford, University of Texas, Aus-600 on July 6, 2020 by guest http://iai.asm.org/ Downloaded from

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Section: Resultsmentioning

confidence: 79%

Siderophore Production by Pathogenic Neisseria spp

Yancey

Finkelstein

1981

Infect Immun

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“…Second, the ColV-B188 plasmid enhanced adhesion in vitro to mouse intestinal epithelium (11). Third, certain CoIV plasmids, but not the ColV,I-K94 plasmid, were found to code for an iron transport system (47,52). Aerobactin was shown to be the siderophore component of this system (50), and the polypeptides involved in aerobactin biosynthesis and transport were identified and mapped by cloning (4; Bindereif et al, submitted for publication).…”

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Aerobactin genes in clinical isolates of Escherichia coli

Bindereif¹,

Neilands²

1985

J Bacteriol

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The location of the aerobactin gene complex on either the chromosome or plasmid was determined in eight aerobactin-positive clinical isolates of Escherichia coli by Southern hybridization analysis, using as probes the cloned aerobactin genes from the ColV-K30 plasmid. The aerobactin genes were in two cases detected on large plasmids, whereas in the other strains the aerobactin genes are most likely located on the chromosome. Restriction mapping revealed only slight variations in the structural genes and an at least 3.4-kilobase-long upstream region conserved in all three plasmid-coded systems. A 7.7-kilobase Hindlll fragment upstream and adjacent to the 16.3-kilobase HindlIl fragment carrying the complete aerobactin system was cloned from the ColV-K30 plasmid. Fine-structure restriction mapping identified the left insertion sequence in the upstream region as IS], in inverted orientation to the IS] element downstream from the aerobactin operon. The upstream and downstream sequences of IS] appear to have perfect homology, as indicated by S1 nuclease resistance of a 760-base-pair DNA duplex formed by both IS) elements. * Corresponding author.Recently we reported a survey of a large number of E. coli clinical isolates for aerobactin synthesis (J. Z. Montgomerie, A. Bindereif, J. B. Neilands, G. Kalmanson, and L. B. Guze, submitted for publication). A high incidence of aerobactin-positive strains (39%) was found. In this paper we determined the genetic location, viz., whether plasmid coded or chromosomal, of the aerobactin biosynthesis and transport determinants in eight aerobactin-positive clinical isolates of E. coli and compare the particular organization of the aerobactin gene complex in these strains. MATERIALS AND METHODSClinical isolates of E. coli. A collection of 54 clinical isolates of E. coli was obtained from J. Z. Montgomerie, Rancho Los Amigos Hospital, Downey, Calif. In addition, the survey included E. coli 0111, a clinical isolate from the Centers for Disease Control, Atlanta, Ga. Recombinant DNA. Restriction enzymes, SI nuclease, DNA polymerase I, and T4 DNA ligase were purchased from Bethesda Research Laboratories (Bethesda, Md.). The large fragment of DNA polymerase I was from New England Biolabs (Beverly, Mass.) The conditions recommended by the supplier were used for restriction enzyme digestions and ligations. The protocols given by Maniatis et al. (26) were followed for most standard recombinant DNA procedures.The cloning vector for the construction of pABN20 was pUC8, 2.7 kilobases (kb) (49). E. coli JM83 [ara A(lac-pro) thi rpsL 4)80dlacZzAM15I was the host for pUC8-derived recombinant plasmids. E. coli JM83 was screened for plasmids by a quick minilysate procedure, which was also used for large-scale isolations of small plasmids (20). For largescale isolations of large plasmids (pColV-K30 and total plasmid DNA from E. coli isolates) the Portnoy procedure was employed (38). Cells from 11 cultures were harvested after 2 to 3 days of growth in Tris-buffered medium (41) with sodium succinate (30 ...

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“…The ability to express the high-affinity system of iron uptake has been correlated with virulence for a variety of microorganisms pathogenic to animals and humans (11). Recently it has been demonstrated that it is the ColV plasmid-directed (12) synthesis in clinical isolates ofEscherichia coli of a hydroxamate-type siderophore (7,13) that accounts, at least in part, for the invasiveness of these organisms. The particular siderophore has been identified as aerobactin (10).…”

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Cloning of the aerobactin-mediated iron assimilation system of plasmid ColV

Bindereif¹,

Neilands²

1983

J Bacteriol

108

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The high-affinity iron assimilation system of plasmid ColV-K30 was cloned on the vector plasmid pPlac. Plasmid pABN1 was isolated by means of sensitivity to cloacin, a bacteriocin using the same outer membrane receptor as ferric aerobactin. Restriction maps were determined for this plasmid and for a subclone, pABN5. Plasmid pABN1 codes for the complete gene complex, whereas plasmid pABN5 encodes only the biosynthetic genes for aerobactin. Regulation of the uptake system by iron is retained in cloned sequences of pABN1.

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Hydroxamate-mediated transport of iron controlled by ColV plasmids

Cited by 74 publications

References 33 publications

Siderophore Production by Pathogenic Neisseria spp

Siderophore Production by Pathogenic Neisseria spp

Aerobactin genes in clinical isolates of Escherichia coli

Cloning of the aerobactin-mediated iron assimilation system of plasmid ColV

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