Hen Egg White Lysozyme Permeabilizes Escherichia coli Outer and Inner Membranes

Derde, Mélanie; Lechevalier-Datin, Valérie; Guérin-Dubiard, Catherine; Cochet, Marie‐Françoise; Jan, Sophie; Baron, Florence; Gautier, Michel; Víe, Véronique; Nau, Françoise

doi:10.1021/jf4029199

Cited by 57 publications

(47 citation statements)

References 44 publications

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“…Membrane permeabilization has been suggested as one of the mechanisms responsible for this activity [8,28]. This assumption was recently confirmed by our group who demonstrated that N-L causes the formation of pores and ion channels in the outer and cytoplasmic membranes, respectively [9,11]. Pore formation due to N-L implies that interactions occur between the protein and the E. coli outer membrane.…”

Section: Discussionmentioning

confidence: 55%

“…It can thus be concluded that N-L reorganizes the LPS monolayer, even if this reorganization remains limited. The reorganization of the LPS monolayer and the LPS/lysozyme complex formation could possibly be the preliminary steps for pore formation by N-L as observed in vivo by Derde et al [9].…”

Section: N-l Interaction With Lps Causes a Slight Reorganization Of Tmentioning

confidence: 74%

“…However, several studies suggest other mechanisms of action against both Gram-positive and Gram-negative bacteria, such as perturbation of DNA or RNA synthesis, activation of autolysin production, and membrane permeabilization [7][8][9][10]. The disruption of both the outer and cytoplasmic membranes of Escherichia coli by native lysozyme has been recently demonstrated in our laboratory [9]. Especially, pore formation in the outer membrane of E. coli has been described [11].…”

Section: Introductionmentioning

confidence: 91%

“…This small enzyme (129 amino acid residues) was for a long time only known for its antimicrobial activity against Grampositive bacteria, due to its muramidase activity [6,7]. However, several studies suggest other mechanisms of action against both Gram-positive and Gram-negative bacteria, such as perturbation of DNA or RNA synthesis, activation of autolysin production, and membrane permeabilization [7][8][9][10]. The disruption of both the outer and cytoplasmic membranes of Escherichia coli by native lysozyme has been recently demonstrated in our laboratory [9].…”

Section: Introductionmentioning

confidence: 99%

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Native lysozyme and dry-heated lysozyme interactions with membrane lipid monolayers: Lateral reorganization of LPS monolayer, model of the Escherichia coli outer membrane

Derde

Nau

Lechevalier-Datin

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Lysozyme is mainly described active against Gram-positive bacteria, but is also efficient against some Gram-negative species. Especially, it was recently demonstrated that lysozyme disrupts Escherichia coli membranes. Moreover, dry-heating changes the physicochemical properties of the protein and increases the membrane activity of lysozyme. In order to elucidate the mode of insertion of lysozyme into the bacterial membrane, the interaction between lysozyme and a LPS monolayer mimicking the E. coli outer membrane has been investigated by tensiometry, ellipsometry, Brewster angle microscopy and atomic force microscopy. It was thus established that lysozyme has a high affinity for the LPS monolayer, and is able to insert into the latter as long as polysaccharide moieties are present, causing reorganization of the LPS monolayer. Dry-heating increases the lysozyme affinity for the LPS monolayer and its insertion capacity; the resulting reorganization of the LPS monolayer is different and more drastic than with the native protein.

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Section: Discussionmentioning

confidence: 55%

Section: N-l Interaction With Lps Causes a Slight Reorganization Of Tmentioning

confidence: 74%

Section: Introductionmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Native lysozyme and dry-heated lysozyme interactions with membrane lipid monolayers: Lateral reorganization of LPS monolayer, model of the Escherichia coli outer membrane

Derde

Nau

Lechevalier-Datin

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…However, lysozyme has been shown to cross this hurdle. 32 Another present defense mechanism in E. coli is the lysozyme inhibitor Ivy, which neutralizes N-L in the periplasm. 36 When N-L reaches the periplasm of E. coli, Ivy binds to N-L.…”

Section: ■ Discussionmentioning

confidence: 99%

Dry-Heating of Lysozyme Increases Its Activity against Escherichia coli Membranes

Derde

Guérin-Dubiard

Lechevalier-Datin

et al. 2014

J. Agric. Food Chem.

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For food as well as for medical applications, there is a growing interest in novel and natural antimicrobial molecules. Lysozyme is a promising candidate for the development of such molecules. This protein is largely studied and known for its muramidase activity against Gram-positive bacteria, but it also shows antimicrobial activity against Gram-negative bacteria, especially when previously modified. In this study, the activity of dry-heated lysozyme (DH-L) against Escherichia coli has been investigated and compared to that of native lysozyme (N-L). Whereas N-L only delays bacterial growth, DH-L causes an early-stage population decrease. The accompanying membrane permeabilization suggests that DH-L induces either larger pores or more pores in the outer membrane as compared to N-L, as well as more ion channels in the inner membrane. The strong morphological modifications observed by optical microscopy and atomic force microscopy when E. coli cells are treated with DH-L are consistent with the suggested disturbances of membrane integrity. The higher hydrophobicity, surface activity, and positive charge induced by dry-heating could be responsible for the increased activity of DH-L on the E. coli membranes.

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Antimicrobial activity of lysozyme isoforms: Key molecular features

et al. 2017

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Increasing bacterial resistance towards antibiotics has stimulated research for novel antimicrobials. Proteins acting on bacterial membranes could be a solution. Lysozyme has been proven active against E. coli by disruption of both outer and cytoplasmic membranes, with dry-heating increasing lysozyme activity. Dry-heated lysozyme (DH-L) is a mixture of isoforms (isoaspartyl, native-like and succinimide lysozymes), giving rise to two questions: what effects does each form have, and which physicochemical properties are critical as regards the antibacterial activity? These issues were investigated by fractionating DH-L, analyzing structural properties of each fraction, and testing each fraction in vivo on bacteria and in vitro on membrane models. Positive net charge, hydrophobicity and molecular flexibility of the isoforms seem key parameters for their interaction with E. coli membranes. The succinimide lysozyme fraction, the most positive, flexible and hydrophobic, shows the highest antimicrobial activity, induces the strongest bacterial membrane disruption and is the most surface active on model lipid monolayers. Moreover, each fraction appears less efficient than DH-L against E. coli, indicating a synergetic cooperation between lysozyme isoforms. The bacterial membrane modifications induced by one isoform could facilitate the subsequent action of the other isoforms.

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Hen Egg White Lysozyme Permeabilizes Escherichia coli Outer and Inner Membranes

Cited by 57 publications

References 44 publications

Native lysozyme and dry-heated lysozyme interactions with membrane lipid monolayers: Lateral reorganization of LPS monolayer, model of the Escherichia coli outer membrane

Native lysozyme and dry-heated lysozyme interactions with membrane lipid monolayers: Lateral reorganization of LPS monolayer, model of the Escherichia coli outer membrane

Dry-Heating of Lysozyme Increases Its Activity against Escherichia coli Membranes

Antimicrobial activity of lysozyme isoforms: Key molecular features

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