Bacteriocin production by members of the genusKlebsiella

Stouthamer, A. H.; Tieze, G. A.

doi:10.1007/bf02097457

Cited by 31 publications

(16 citation statements)

References 10 publications

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“…However, our results show that these strains can be separated into two distinct groups, based on bacteriocin production, maceration of onion slices, hydrolysis of low pH pectate agar and plasmid profile. Bacteriocin production is more stable as an epidemiological marker than bacteriocin sensitivity (Farmer, 1972a, b) and has been used as an epidemiological tool for a number of Gram-negative bacteria (Abbott & Shannon, 1958;Farmer, 1972a, b ;Gillies & Govan, 1966;Stouthamer & Tieze, 1966;Vidaver et al, 1972). The production patterns obtained with the Hines strains as indicators clearly allowed differentiation between the plant isolates of P. cepacia and those of clinical origin.…”

Section: Discussionmentioning

confidence: 99%

Bacteriocin, Plasmid and Pectolytic Diversity in Pseudomonas cepacia of Clinical and Plant Origin

Gonzalez

Vidaver

1979

Journal of General Microbiology

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161Pseudomonas cepacia strains of plant and clinical origin were compared with the type strains of P. cepacia, P. kingii and P. multivorans. Conventional biochemical tests and antibiotic sensitivity patterns supported the previous proposals of synonymy between P. cepacia, P. kingii and P. multivorans. However, bacteriocin production patterns, onion maceration tests and hydrolysis of low pH pectate agar clearly differentiated strains of clinical and plant origin into two distinct groups; these tests may therefore be helpful in epidemiological studies. In contrast, plant and clinical strains were of equal lethality to mice. Agarose gel electrophoresis indicated the presence of one or more plasmids (molecular weights 9 x lo6 to 120 x lo6) in 15 out of 16 strains of both types examined.

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Section: Discussionmentioning

confidence: 99%

Bacteriocin, Plasmid and Pectolytic Diversity in Pseudomonas cepacia of Clinical and Plant Origin

Gonzalez

Vidaver

1979

Journal of General Microbiology

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“…Purified cloacin DF13 was prepared from the same strain by QAE-Sephadex chromatography in the presence of 6 M urea as described previously [3]. Purified immunity protein was prepared from Escherichia coli P678-54 (Clo DF13-Rep 3) as described previously [8]. The sensitive strain Klebsiella edwardsii var.…”

Section: Bacterial Strainsmentioning

confidence: 99%

“…Fig. 3 (e and f) shows an analysis of cloacin and of immunity protein which have been isolated and purified as described previously [3,8].…”

Section: Fig 1 Cm-sephudeu Chromatography O J the Crude Bacteriocinmentioning

confidence: 99%

Purification and Characterization of a Complex between Cloacin and Its Immunity Protein Isolated from Enterobacter cloacae (Clo DF13). Dissociation and Reconstitution of the Complex

Graaf¹,

Klaasen-Boor²

1977

Eur J Biochem

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Cells of Enterobacter cloacae (Clo DF13) produce a bacteriocin which is characterized by its very effective killing activity against sensitive bacteria. Purification and characterization of the excreted bacteriocin has revealed that this bacteriocin consists of an equimolar complex of two plasmidspecific gene products: the cloacin and its inhibitor the immunity protein. Dissociation of the complex by treatment with sodium dodecylsulfate induces the endonucleolytic activity of the cloacin but strongly reduces the killing activity. The purified complex possesses no activity in vitro. Both cloacin and immunity protein isolated from the complex were functionally identical to cloacin and immunity protein purified from the bacteriocinogenic cells by other methods. Reconstitution of the complex results in a partial restoration of killing activity.

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“…Cloacin DF13 is a bacteriocin produced by strains of Enterobacter cloacae that harbor plasmid CloDF13 (21). Killing of sensitive enteric bacteria by cloacin DF13 involves three distinct stages (13,25): binding to a specific surface receptor protein, transport of an active fragment of the bacteriocin molecule through the cell envelope, and endoribonucleolytic cleavage of 16S rRNA, resulting in defective protein synthesis.…”

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confidence: 99%

Sensitivity of Escherichia coli to cloacin DF13 involves the major outer membrane protein OmpF

Wooldridge

Williams

1991

J Bacteriol

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Fourteen spontaneous cloacin DF13-insensitive mutants of an Escherichia coli strain expressing the aerobactin-cloacin DF13 receptor protein IutA were isolated. The mutants fell into three classes on the basis of outer membrane profiles analyzed by electrophoresis in denaturing polyacrylamide gels. The most frequent class lacked the lutA protein and was unable to bind cloacin DF13 or aerobactin. A second class of mutants had lost protein species corresponding in size to the porin proteins OmpF and OmpC. To determine which porin was required for the bactericidal activity of cloacin DF13, defined strains with mutations at the ompB (ompR envZ) locus were transformed with a recombinant plasmid carrying the iutA gene and screened for cloacin DF13 sensitivity. OmpF-strains, whether OmpC+ or OmpC-, were insensitive to cloacin DF13, indicating involvement of the OmpF protein in cloacin DF13 killing. An OmpC-OmpF+ strain, on the other hand, was more sensitive than the wild-type parent strain, probably because of compensatory overexpression of OmpF. The third class of cloacin DF13-insensitive mutant had lost an outer membrane protein of approximately 31 kDa. The nature and function of this protein are not yet known, but it is not the protease OmpT. Mutants of classes 2 and 3 bound cloacin DF13 and aerobactin as effectively as the cloacin DF13-sensitive parental strain, indicating that they remained IutA+. We propose that these mutants (more accurately described as cloacin DF13 tolerant) are defective in translocation of the active portion of cloacin DF13 across the bacterial membranes.Cloacin DF13 is a bacteriocin produced by strains of Enterobacter cloacae that harbor plasmid CloDF13 (21). Killing of sensitive enteric bacteria by cloacin DF13 involves three distinct stages (13, 25): binding to a specific surface receptor protein, transport of an active fragment of the bacteriocin molecule through the cell envelope, and endoribonucleolytic cleavage of 16S rRNA, resulting in defective protein synthesis. The cloacin DF13 receptor in several enterobacterial species also acts as a receptor for the hydroxamate siderophore aerobactin (2,14,25). Thus, strains of Escherichia coli that utilize aerobactin as a source of iron, a category that includes many pathogenic isolates (3,26), are sensitive to cloacin DF13 because they express the 74-kDa outer membrane aerobactin receptor protein lutA (2). Killing of E. coli by cloacin DF13, unlike many other bacteriocins, is not dependent on the cytoplasmic membrane protein TonB (20); the aerobactin receptor is therefore the only envelope-associated protein in E. coli reported to date to be required for cloacin DF13 activity. In this paper we show that the major outer membrane protein OmpF, and possibly an outer membrane protein of 31 kDa, are also essential for the lethal action of cloacin DF13. MATERIALS AND METHODSBacteria and culture conditions. The bacterial strains used in this study are described in Table 1. Plasmid pLG141 comprises a 6.5-kb BamHI fragment of plasmid that includes the...

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Bacteriocin production by members of the genusKlebsiella

Cited by 31 publications

References 10 publications

Bacteriocin, Plasmid and Pectolytic Diversity in Pseudomonas cepacia of Clinical and Plant Origin

Bacteriocin, Plasmid and Pectolytic Diversity in Pseudomonas cepacia of Clinical and Plant Origin

Purification and Characterization of a Complex between Cloacin and Its Immunity Protein Isolated from Enterobacter cloacae (Clo DF13). Dissociation and Reconstitution of the Complex

Sensitivity of Escherichia coli to cloacin DF13 involves the major outer membrane protein OmpF

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