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

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

doi:10.1016/j.bbamem.2014.10.026

Cited by 27 publications

(13 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The negatively charged molecule lipopolysaccharide in the outer membrane of gram-negative bacteria can attract cationic antimicrobial proteins [ 64 ]. In fact, the presence of lipopolysaccharide in in vitro–generated lipid monolayers is sufficient to promote the insertion of lysozyme [ 65 ]. However, while reducing the negative charge of lipopolysaccharide generally increases the resistance of gram-negative bacteria to cationic antimicrobial proteins [ 64 ], the degree to which this affects gram-negative resistance to lysozyme is largely unknown.…”

Section: Mechanisms Of Bacterial Lysozyme Resistancementioning

confidence: 99%

From bacterial killing to immune modulation: Recent insights into the functions of lysozyme

2017

View full text Add to dashboard Cite

Lysozyme is a cornerstone of innate immunity. The canonical mechanism for bacterial killing by lysozyme occurs through the hydrolysis of cell wall peptidoglycan (PG). Conventional type (c-type) lysozymes are also highly cationic and can kill certain bacteria independently of PG hydrolytic activity. Reflecting the ongoing arms race between host and invading microorganisms, both gram-positive and gram-negative bacteria have evolved mechanisms to thwart killing by lysozyme. In addition to its direct antimicrobial role, more recent evidence has shown that lysozyme modulates the host immune response to infection. The degradation and lysis of bacteria by lysozyme enhance the release of bacterial products, including PG, that activate pattern recognition receptors in host cells. Yet paradoxically, lysozyme is important for the resolution of inflammation at mucosal sites. This review will highlight recent advances in our understanding of the diverse mechanisms that bacteria use to protect themselves against lysozyme, the intriguing immunomodulatory function of lysozyme, and the relationship between these features in the context of infection.

show abstract

Section: Mechanisms Of Bacterial Lysozyme Resistancementioning

confidence: 99%

From bacterial killing to immune modulation: Recent insights into the functions of lysozyme

2017

View full text Add to dashboard Cite

show abstract

“…This explanation is also assumed for the interface-active apolipoproteins A-I and A-II at the lipid-water interface. The average residue hydrophobicity and the probable helical structure of these types of proteins may be the key factor for this binding affinity with the phospholipid monolayer at the air-water interface [23,24]. Also, the same interaction procedure has been discussed by Donald and Patterson [25] when studying the adsorption and insertion of β-lactoglobulin from solution into the lipid monolayer at the airwater interface.…”

Section: Lipid Solution and Monolayer Preparation 23 Lipoprotein Solmentioning

confidence: 87%

Adsorption kinetics of low-density lipoproteins with Langmuir monolayer

Khattari

2016

J Biol Phys

View full text Add to dashboard Cite

The present work utilizes the Langmuir monolayer technique to detect the adsorption kinetics of native low-density lipoproteins and their oxidized form with the lipid monolayer. We found that low-density lipoproteins and oxidized low-density lipoproteins are able to penetrate the LM up to pressure π = 9.9 and 11.6 mN/m. Also, the adsorption constants of both particles were found to depend strongly on the monolayer initial pressure. It is found that less compressed lipid monolayers could accommodate more native low-density lipoproteins than the oxidized ones due their higher binding affinity toward monolayers. The probable α-helical regions along the apoproteinB-100 secondary structure and average hydrophobicity could explain partially their adsorption kinetics into lipid monolayers. This simplified 'in vitro' study of low-density lipoproteinmonolayer interaction may serve as a step further to understand the mechanism and bioactivity of the atherosclerotic process. Also, it may shed light on the oxidized low-density lipoprotein's role in plaque formation in the innermost arterial wall in blood vessels. Keywords Langmuir monolayer . Atherosclerosis . LDL oxidation . Adsorption kineticsAtherosclerosis is a complex chronically developing human disease initiated by and progressing as a result of excessive accumulation of lipids (e.g., mostly cholesterol in human blood) in the smooth arterial wall [1][2][3]. Cardiovascular disease is first distinguishable by a fatty streak, which is lipid-rich macrophages and T lymphocytes trapped by the artery wall (i.e., intima) [4]. As oxidization continues, fatty steaks decompose to polyunsaturated

show abstract

“…Gram-positive bacteria have a thick cell wall composed of up to 40 layers of peptidoglycan, which is very sensitive to lysozyme [ 26 ], while Gram-negative bacteria typically have only a single layer of peptidoglycan surrounded by an asymmetric membrane bilayer, which is thought to render Gram-negative bacteria naturally impermeable to lysozyme, and thus resistant to its effects [ 26 ]. However, recent evidence indicates that lysozyme can interact with the negatively charged membrane lipid bilayers leading to protein aggregation and membrane fusion [ 27 ], and can permeabilize the outer and inner membranes of an E. coli mutant ML-35p by inducing the formation of large pores [ 6 , 28 ]. This suggests that the physical barrier afforded by the outer membrane of Gram-negative bacteria might not be the main reason responsible for their greater resistance to lysozyme.…”

Section: Discussionmentioning

confidence: 99%

O-specific polysaccharide confers lysozyme resistance to extraintestinal pathogenic Escherichia coli

et al. 2018

View full text Add to dashboard Cite

Extraintestinal pathogenic Escherichia coli (ExPEC) is the leading cause of bloodstream and other extraintestinal infections in human and animals. The greatest challenge encountered by ExPEC during an infection is posed by the host defense mechanisms, including lysozyme. ExPEC have developed diverse strategies to overcome this challenge. The aim of this study was to characterize the molecular mechanism of ExPEC resistance to lysozyme. For this, 15,000 transposon mutants of a lysozyme-resistant ExPEC strain NMEC38 were screened; 20 genes were identified as involved in ExPEC resistance to lysozyme—of which five were located in the gene cluster between galF and gnd, and were further confirmed to be involved in O-specific polysaccharide biosynthesis. The O-specific polysaccharide was able to inhibit the hydrolytic activity of lysozyme; it was also required by the complete lipopolysaccharide (LPS)-mediated protection of ExPEC against the bactericidal activity of lysozyme. The O-specific polysaccharide was further shown to be able to directly interact with lysozyme. Furthermore, LPS from ExPEC strains of different O serotypes was also able to inhibit the hydrolytic activity of lysozyme. Because of their cell surface localization and wide distribution in Gram-negative bacteria, O-specific polysaccharides appear to play a long-overlooked role in protecting bacteria against exogenous lysozyme.

show abstract

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

Cited by 27 publications

References 36 publications

From bacterial killing to immune modulation: Recent insights into the functions of lysozyme

From bacterial killing to immune modulation: Recent insights into the functions of lysozyme

Adsorption kinetics of low-density lipoproteins with Langmuir monolayer

O-specific polysaccharide confers lysozyme resistance to extraintestinal pathogenic Escherichia coli

Contact Info

Product

Resources

About