Abortive Infection by Bacteriophage Me1 of Escherichia coli K12 Strains Bearing the Plasmid ColV, I-K94

Reakes, C. F. L.; Gann, Alexander; Rossouw, F.T.; Rowbury, R. J.

doi:10.1099/0022-1317-68-2-263

Cited by 3 publications

(4 citation statements)

References 28 publications

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“…The aim was, firstly, to compare such plasmids to ColV,I-K94 with respect to restriction digest pattern, colicin production-immunity, transfer properties, effects on phage Me1 multiplication (Reakes et al 1987), and encoding of the VmpA protein, and secondly, to ascertain whether any of these specific plasmid characteristics correlated with ability of the plasmid to suppress the inhibitor sensitivities of ompA mutants.…”

Section: Suppression Of Antibiotic Sensitivity By Colvi-k94mentioning

confidence: 99%

“…All of the clinical COW+ strains were resistant to plaquing by several tested phages (MS2, T4, Mel, PI). Because of the inhibition of phage Me1 development by ColV,I-K94 (de Pacheco et al 1985;Reakes et al 1987), the ability of this phage to attach to the clinical ColV+ strains was tested. Only 3/220 showed attachment.…”

Section: Suppression Of Antibiotic Sensitivity By Colvi-k94mentioning

confidence: 99%

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Suppression by the ColV,I-K94 plasmid of inhibitor sensitivities in ompA mutants of Escherichia coli

Reakes¹,

Deeney²,

Goodson³

et al. 1988

Can. J. Microbiol.

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A series of ompA mutants derived from Escherichia coli K12 strains showed increased sensitivity (compared with the ompA+ parents) to aminoglycoside antibiotics and to other cationic agents including polymyxin B. One tested mutant also showed increased sensitivity to nafcillin and fusidic acid, but not to the hydrophilic ampicillin. All these inhibitor sensitivities in the ompA mutants were suppressed by ColV, I-K94 and by certain other ColV plasmids, but not by any of the other tested large plasmids. Suppression correlated with the production of the VmpA protein, but transfer and colicin components were not needed for suppression. Further comparison of the ompA and vmpA genes and their products was made and it indicated that there is little if any homology between the genes, that the synthesis of their products is regulated by quite different mechanisms, and that regions of these gene products exposed at the cell surface show different susceptibility to protease attack after denaturation.

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Section: Suppression Of Antibiotic Sensitivity By Colvi-k94mentioning

confidence: 99%

Section: Suppression Of Antibiotic Sensitivity By Colvi-k94mentioning

confidence: 99%

Suppression by the ColV,I-K94 plasmid of inhibitor sensitivities in ompA mutants of Escherichia coli

Reakes¹,

Deeney²,

Goodson³

et al. 1988

Can. J. Microbiol.

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“…Colicins undoubtedly serve a number of functions within the E. coli population, but their ecological role is still not clear (Cascales et al, 2007;Riley & Wertz, 2002). It has been previously reported that ColIb and ColV are able to exert an inhibitory effect against T-odd bacteriophage and Me1 bacteriophage, respectively (Duckworth & Pinkerton, 1988;Reakes et al, 1987). E. coli containing ColE7-K317 shows limited protection against bacteriophage M13K07 and l infection (Lin et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Interaction of colicin E7 with the major coat protein (g8p) may confer limited protection on colicinogenic Escherichia coli against M13 bacteriophage infection

et al. 2010

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Colicin release provides producer strains with a competitive advantage under certain circumstances. We found that propagation of M13 bacteriophage in cells producing colicin E7 is impaired, without alteration in the efficiency of bacteriophage adsorption, as compared with nonproducing cells. In contrast to the protective effect of the colicin against M13 bacteriophage infection, the endogenously expressed colicin does not confer limited protection against transfection with M13 bacteriophage DNA. Furthermore, it was found that the translocationreceptor-binding domain and toxicity domain of the colicin are able to interact with the M13 major coat protein, g8p, during bacteriophage infection. Based on these observations, we propose that interaction between colicin E7 and g8p during infection interferes with g8p depolymerizing into the cytoplasmic membrane during bacteriophage DNA penetration, thus resulting in the limited protection against M13 bacteriophage infection.

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“…Recent studies of ColV ÷ strains (Reakes et al, 1987) have indicated that plasmid ColV,I-K94 causes abortive infections by the T4-1ike phage Mel. During studies of sensitivity to further phages, it was found that phage P lvir was unable to form plaques on ColV,I-K94 ÷ strains.…”

Section: Introductionmentioning

confidence: 99%

Altered Phage P1 Attachment to Strains of Escherichia Coli Carrying the Plasmid ColV,I-K94

Goodson

Rowbury

1987

Journal of General Virology

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Abortive Infection by Bacteriophage Me1 of Escherichia coli K12 Strains Bearing the Plasmid ColV, I-K94

Cited by 3 publications

References 28 publications

Suppression by the ColV,I-K94 plasmid of inhibitor sensitivities in ompA mutants of Escherichia coli

Suppression by the ColV,I-K94 plasmid of inhibitor sensitivities in ompA mutants of Escherichia coli

Interaction of colicin E7 with the major coat protein (g8p) may confer limited protection on colicinogenic Escherichia coli against M13 bacteriophage infection

Altered Phage P1 Attachment to Strains of Escherichia Coli Carrying the Plasmid ColV,I-K94

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