Permeability of lipopolysaccharide-deficient (rough) mutants of <i>Salmonella typhimurium</i> to antibiotics, lysozyme, and other agents

Sanderson, Kenneth E.; MacAlister, T J; Costerton, J. W.; Cheng, K.-J.

doi:10.1139/m74-176

Cited by 111 publications

(68 citation statements)

References 22 publications

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“…Thus, in contrast to the previous findings (6,22,27), all of these recent observations are consistent with the possibility that both the protein and LPS moieties of the outer membrane contribute to the normal functioning of the outer membrane as a `permeability barrier' in gram-negative bacteria.…”

Section: Discussionsupporting

confidence: 87%

“…It has been suggested (3)(4)(5), therefore, that the altered LPS structure of the outer membrane of these mutants facilitates the release of periplasmic enzymes into the growth medium. In addition, the sensitivity of these mutant strains to phages, antibiotics (6,21), dyes, detergents (23)(24)(25)(26), lysozyme (22,27), and dicyclohexylcarbodiimide (28) has been attributed solely to a defect in the polysaccharide structure of the LPS (see for further discussion Ref. 29).…”

Section: Discussionmentioning

confidence: 99%

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Leakage of Periplasmic Enzymes From Cells of Heptose-Deficient Mutants of Escherichia Coli, Associated With Alterations in the Protein Component of the Outer Membrane

Singh

Reithmeier

1975

J. Gen. Appl. Microbiol.

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Large amounts of alkaline phosphatase and 2,3-cyclic phosphodiesterase were released into the culture medium during the active growth of heptose-deficient mutants of Escherichia coli NS1 to NS3, but no periplasmic enzymes were released from cells of the wild type strain JE. The NS mutants were hyper-sensitive to lysozyme, ethylenediaminetetraacetate (EDTA), sodium deoxycholate (DOC), sodium dodecyl sulfate (SDS), and Triton X100; the sensitivity to detergent was increased several fold when the treatment was carried out in the presence of potassium cyanide. The wild type strain was not sensitive to lysozyme or detergents, even in the presence of KCN. Both the wild type and mutant strains were sensitive to colicins, El, E2, E3, G, H, and K, and to phages T2, T3, T6, and BF23, but they were resistant to phages P22, FO, Ffm, 6SR, Br2, Br60, C21, and T5. Unlike the wild type strain, the NS mutants were resistant to phages T4, T7, and Br10. A comparison of the protein composition of the outer membrane of wild type and NS1 strains indicated that one major protein species of molecular weight (mol. wt.) 50,000 was absent while two other proteins of mol. wt. 40,000 and 33,400 were present only in reduced amounts in the outer membrane of the NS 1 mutant. These observations suggest that both the polysaccharide and protein components of the outer membrane of E, toll participate in the normal functioning of the outer membrane as a `permeability barrier .' Under normal growth conditions the chia coli and Salmonella typhimurium (1), 109`p eriplasmic leaky' mutants of Escheriand the lactose transport-negative (y-)

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Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Leakage of Periplasmic Enzymes From Cells of Heptose-Deficient Mutants of Escherichia Coli, Associated With Alterations in the Protein Component of the Outer Membrane

Singh

Reithmeier

1975

J. Gen. Appl. Microbiol.

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“…Sensitivity to antibiotics. Many mutants with altered cell envelopes show changes in sensitivity to various antibiotics (Raetz & Foulds, 1977;Sanderson et al, 1974;Tamaki & Matsuhashi, 1973). Approximately 40 different antibiotics were tested against strain UB1005 and mutants DC7 and DC11.…”

Section: R E S U L T Smentioning

confidence: 99%

Altered Phospholipid Composition in Mutants of Escherichia coli Sensitive or Resistant to Organic Solvents

Clark¹,

Beard

1979

Journal of General Microbiology

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Mutants of Escherichia coli with altered resistance to low molecular weight organic solvents were isolated. Solvent-resistant mutants showed a decrease in the ratio of phosphatidylethanolamine to the anionic phospholipids (phosphatidylglycerol and cardiolipin) relative to the wild-type, whereas solvent-sensitive strains showed an increase. Reversion studies on representative mutants demonstrated that the phenotypic response to solvents and the changes in phospholipid composition were genetically associated. The fatty acid and lipopolysaccharide compositions of the various mutants showed no significant differences from the parental strain. The lesions in two of the solvent-sensitive mutants (DC7 and DC9) and one of the resistant mutants (DC11) were mapped by cotransduction with phage P1 and shown to lie very close to thepss locus at 56 min on the Escherichia coli map. I N T R O D U C T I O NAlcohols and other low molecular weight solvents have long been known to inhibit the growth of bacteria (Dagley et al., 1950). Low concentrations of solvents are reversible in action whereas higher concentrations are lethal (Harold, 1970). The target for solvents appears to be the lipid bilayer of the cell membranes (Hugo, 1967). Low concentrations of solvents dissolve into lipid bilayers, increasing the bilayer fluidity (Hill, 1974), whereas higher concentrations cause irreversible disruption and, eventually, lysis (Harold, 1970;Hugo, 1967). These observations suggested that mutants with an altered sensitivity to organic solvents might have an altered lipid composition which would change their membrane fluidity. We therefore isolated mutants of Escherichia coli K12 with altered sensitivity to ethanol and examined their lipid compositions. METHODSBacterial strains and media. Bacterial strains are listed in Table 1. Strain UB1005 is a spontaneous nalidixic acid-resistant derivative of W1655F- (Bachmann, 1972) and is the parent of mutants DC7 to DCl1. Strain KY2670 and its phenylethyl alcohol-resistant/azide-sensitive derivative KY2671 were received from D r T. Yura (Kyoto University, Japan).The nutrient broth has been described previously (Beard & Conolly, 1975 It was supplemented with necessary L-amino acids at 20 pg ml-I. Solid media contained 1.65 yo (w/v) agar. Mutagenesis and isolation of mutants. Mutagenesis was performed with

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“…The degree of effectiveness against gram-negative bacteria of many antibacterial systemns, including cellutlar and humoral host defenses and antibiotics, depends largely on the physicochemical properties of this outer membrane (6)(7)(8)(9)(10). These properties imainly appear determined by the length of the polysaccharide chain of the outer menmbrane lipopolysaccharides (LPS) (11)(12)(13).…”

Section: Introductionmentioning

confidence: 99%

Resistance of Gram-negative Bacteria to Purified Bactericidal Leukocyte Proteins

Weiss¹,

Beckerdite-Quagliata²,

Elsbach³

1980

J. Clin. Invest.

112

105

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A B S T R A C T The sensitivitv or resistance of gramnegative bacteria to antibacterial systemis appears to be related to the length of the saccharide chain of the bacterial envelope lipopolysaccharides (LPS). To explore this relationship further, we miade use of two bactericidal, miembrane-active cationic proteins, recently purified to near homiogeneity, one from human and one fromi rabbit polymnorphonuclear leukocytes (PNIN). We have studied the effects of these two closely simiilar proteins on strains of Salmiionella typhinuriutrm and Escherichia coli, each separate strain differing in the saccharide chain length of its outer memlbrane LPS. Binding of these proteins to the bacterial outer membrane is required for killing, and is accompianied by an almost immnediate increase in outer memnbrane permeability to normally impermieant actinomycin D. Sensitivity to the bactericidal and permeability-increasing activities of the human and rabbit proteins increases with decreasing LPS-saccharide chain length (chemiotype: [S < Ra < Rb3 < Rc < Rd1]). S. typhimurium G-30 and E. coli J5, mutant strains lacking UDP-galactose-4-epimnerase, synthesize incomplete LPS (chemotype Rc) whein grown without galactose, and are then as sensitive to both PMIN proteins as the S. typhimurium strains 395 RIO (Rd1) and R5 (Rb3). However, when these imutants are grown with galactose, they synthesize complete LPS (chemiotype S) and exhibit nearly the same relative insensitivity as the smooth strains S. typhimurium 395 NIS aind E. coli 0111:B4.

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Permeability of lipopolysaccharide-deficient (rough) mutants of Salmonella typhimurium to antibiotics, lysozyme, and other agents

Cited by 111 publications

References 22 publications

Leakage of Periplasmic Enzymes From Cells of Heptose-Deficient Mutants of Escherichia Coli, Associated With Alterations in the Protein Component of the Outer Membrane

Leakage of Periplasmic Enzymes From Cells of Heptose-Deficient Mutants of Escherichia Coli, Associated With Alterations in the Protein Component of the Outer Membrane

Altered Phospholipid Composition in Mutants of Escherichia coli Sensitive or Resistant to Organic Solvents

Resistance of Gram-negative Bacteria to Purified Bactericidal Leukocyte Proteins

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