Hydrolysis of Phospholipids by phospholipase C in intact cells of wild‐type and envelope mutants of <i>Escherichia coli K12</i>

Stárková, Zdena; Bonnaveiro, N; Stárka, J.

doi:10.1016/0014-5793(81)81134-9

Cited by 9 publications

(3 citation statements)

References 16 publications

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“…Heat treatment of E. coli cells might also induce a similar disturbance of the outer membrane structure, as shown by the sensitization to phospholipase C added externally in this study, although the penetration of phospholipase C into the periplasmic space, followed by the degradation of lipids in the cytoplasmic membrane, cannot be ruled out. The degree of phospholipid hydrolysis in cells heated for 30 min in HEPES and Tris-Mg buffers were comparable to those (30 to 50%) in some mutants deficient in the cell envelope structure of E. coli (30) and S. typhimurium (12). In Tris buffer, however, a large amount (66%) of the phospholipids was hydrolyzed 30 min after heat treatment, despite the absence of cell lysis.…”

Section: Discussionmentioning

confidence: 61%

Destruction of the outer membrane permeability barrier of Escherichia coli by heat treatment

Tsuchido¹,

Katsui²,

Takeuchi³

et al. 1985

Appl Environ Microbiol

182

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Heat treatment of a wild-type Escherichia coli strain at 55 degrees C in 50 mM Tris-hydrochloride buffer with or without 10 mM magnesium sulfate or HEPES (N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid) buffer at pH 8.0 caused an increase in cell surface hydrophobicity. By determining the location of n-hexadecane droplets attached to cells by phase-contrast microscopy, the septal and polar regions of heated cells appeared to become the most frequently hydrophobic. Some of the lipopolysaccharide molecules in the outer membrane were released from heated cells, and the cells became susceptible to the hydrolytic action of added phospholipase C. Heat-treated cells also became permeable to the hydrophobic dye crystal violet, which was added externally. The release of part of the outer membrane by heat treatment appeared to bring about the disorganization of the outer membrane structure and, as a consequence, to result in the partial disruption of the permeability barrier function of the outer membrane. Tris was found to enhance damage to the outer membrane by heat.

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Section: Discussionmentioning

confidence: 61%

Destruction of the outer membrane permeability barrier of Escherichia coli by heat treatment

Tsuchido¹,

Katsui²,

Takeuchi³

et al. 1985

Appl Environ Microbiol

182

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“…Both are very susceptible to benzylpenicillin, methicillin, and cloxacillin, and both are practically resistant to rifampin. The drug susceptibility phenotypes of the acrA (5), the envA (7,8,19), and especially the envC (22,24) mutants have been only partially evaluated, so comparisons are less easily made. However, it appears that the SS-B mutant is much more susceptible than the acrA mutant of E. coli.…”

Section: Resultsmentioning

confidence: 99%

Antimicrobial susceptibility of Salmonella typhimurium carrying the outer membrane permeability mutation SS-B

Vaara

1990

Antimicrob Agents Chemother

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The antibiotic susceptibility profile of Salmonella typhimurium SS-B, a mutant susceptible to some antimicrobial agents, was studied in detail. Twenty-eight agents were tested, and eleven of these had MICs significantly lower (32- to greater than 250-fold) for the SS-B strain than for its parent. The drugs were generally hydrophobic or amphiphilic. Polymyxin B nonapeptide, which has a known outer membrane permeabilizing action, further reduced the MIC of several of these agents for the SS-B strain by a factor of approximately 10 to 30. In most cases, the resulting MICs were lower than the corresponding MICs for the parent strain grown in the presence of polymyxin B nonapeptide. In addition, the hydrophobic fluorescent probe N-phenyl naphthylamine was rapidly embedded in the membranes of the SS-B strain but was poorly embedded in those of the parent strain.

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“…Thus enoC was considered to be a pleiotropic mutation. Among the abnormalities were hypersensitivity to dyes, detergents, phospholipase C and some antibiotics, leakiness and alterations in phospholipid composition and metabolism [2,3]. The question arose as to whether the PM61 EnvC phenotype reflected a composite of several mutations or a single pleiotropic mutation.…”

Section: Introductionmentioning

confidence: 99%

The EnvC phenotype and its expression in various Escherichia coli K12 strains

Karibian¹

1985

FEMS Microbiology Letters

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The septation-deficient mutant of Escherichia coli K12, PM61 envC, has been reported to have many membrane-related anomalies. To distinguish between real pleiotropy and a multimutational phenotype, the envC region was co-transduced with a selectable marker into 4 strains and the phenotypes of the transductants examined. It was found that (1) lysophosphatidylethanolamine accumulation did not cause EnvC morphology, nor was it caused by the envC lesion; (2) a low phosphatidylglycerol/diphosphatidylglycerol ratio (PG/DPG), hypersensitivity to tetracycline and resistance to novobiocin were dissociable from envC by transduction, but hypersensitivity to deoxycholate was not; (3) septation deficiency was expressed to variable degrees in different host strains. Thus, PM61 bears several envelope-related mutations in the 81 min region. The transduction results also suggested that the envC site is slightly upstream from cysE.

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Hydrolysis of Phospholipids by phospholipase C in intact cells of wild‐type and envelope mutants of Escherichia coli K12

Cited by 9 publications

References 16 publications

Destruction of the outer membrane permeability barrier of Escherichia coli by heat treatment

Destruction of the outer membrane permeability barrier of Escherichia coli by heat treatment

Antimicrobial susceptibility of Salmonella typhimurium carrying the outer membrane permeability mutation SS-B

The EnvC phenotype and its expression in various Escherichia coli K12 strains

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