Lysozyme interactions with phospholipid vesicles: relationships with fusion and release of aqueous content

Posse, E; Arcuri, Beatriz F. de; Morero, Roberto D.

doi:10.1016/0005-2736(94)90338-7

Cited by 49 publications

(34 citation statements)

References 18 publications

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“…Subsequently, the solution was dialyzed at 4°C against 20 mM HEPES, pH 7.4. The degree of labeling was estimated using extinction coefficients of 7 Protein labeling with SeTau-647-di-NHS. Stock solution of Lz was made by dissolving 1 mg of the protein in 1 ml of borate buffer, pH 9.…”

Section: Lysozyme Labeling With Fluorescent Labelsmentioning

confidence: 99%

“…Discovered by Alexander Fleming in 1922, lysozyme was the first protein whose three-dimensional structure was characterized at atomic resolution [1]. Owing to its well-defined geometry and physicochemical properties Lz represents an attractive model in approaching a broad spectrum of fundamental problems including protein adsorption at interfaces [2], lipid-protein interactions [3][4][5], membrane fusion [6,7], protein folding, aggregation and amyloid fibrillogenesis [8][9][10]. A number of studies provide evidence for pronounced lipid-associating ability of lysozyme [11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

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Modulation of physiological and pathological activities of lysozyme by biological membranes

Trusova

2012

Cellular and Molecular Biology Letters

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Abstract:The molecular details of interactions between lipid membranes and lysozyme (Lz), a small polycationic protein with a wide range of biological activities, have long been the focus of numerous studies. The biological consequences of this process are considered to embrace at least two aspects: i) correlation between antimicrobial and membranotropic properties of this protein, and ii) lipid-mediated Lz amyloidogenesis. The mechanisms underlying the lipid-assisted protein fibrillogenesis and membrane disruption exerted by Lz in bacterial cells are believed to be similar. The present investigation was undertaken to gain further insight into Lz-lipid interactions and explore the routes by which Lz exerts its antimicrobial and amyloidogenic actions. Binding and Förster resonance energy transfer studies revealed that upon increasing the content of anionic lipids in lipid vesicles, Lz forms aggregates in a membrane environment. Total internal reflection fluorescence microscopy and pyrene excimerization reaction were employed to study the effect of Lz on the structural and dynamic properties of lipid bilayers. It was found that Lz induces lipid demixing and reduction of bilayer free volume, the magnitude of this effect being much more pronounced for oligomeric protein.

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Section: Lysozyme Labeling With Fluorescent Labelsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Modulation of physiological and pathological activities of lysozyme by biological membranes

Trusova

2012

Cellular and Molecular Biology Letters

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“…[1][2][3] It is also important for food storage because a large number of foods exist in the form of emulsion. Proteins are often used as emulsifiers for food stabilization.…”

Section: Introductionmentioning

confidence: 99%

Penetration and Saturation of Lysozyme in Phospholipid Bilayers

et al. 2007

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We show that the combination of X-ray reflectivity, tryptophan fluorescence spectrum, and fluorescence quenching by bromine provides a useful tool to probe the location of lysozyme in lipid bilayers. To this end, we prepare lamellar complexes composed of phospholipids and lysozyme on solid surfaces using a solutioncasting method. The proteins lie spontaneously between adjacent bilayers in the complexes. The results indicate that lysozyme may penetrate into the lipid bilayers. But the penetration depth is very shallow, and the tryptophan residues do not penetrate beyond the interface between the hydrocardon core and the headgroup region of the lipid bilayer. The penetration becomes saturated when more proteins are incorporated into the lamellar complex. The excess proteins stay in the interlamellar aqueous layers.

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“…Lysozyme is an antimicrobial enzyme widely distributed in nature and is found in mammalian tissues and secretions, insects, plants, bacteria, and viruses (1). Besides its antimicrobial activity, lysozyme has many other functions including inactivation of certain viruses (2), surveillance of membranes of mammalian cells (3), enhancing phagocytic activity of polymorphonuclear leukocytes (4) and macrophages (5), stimulation of monocytes (6), antitumor activity (7), and induction of fusion of phospholipids vesicles (8).…”

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confidence: 99%

A Helix-Loop-Helix Peptide at the Upper Lip of the Active Site Cleft of Lysozyme Confers Potent Antimicrobial Activity with Membrane Permeabilization Action

Ibrahim¹,

Thomas²,

Pellegrini³

2001

Journal of Biological Chemistry

260

203

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Recently, we have found that partially unfolded lysozyme exerts broad spectrum antimicrobial action in vitro against Gram-negative and Gram-positive bacteria independent of its catalytic activity. In parallel, an internal peptide (residues 98 -112) of hen egg white lysozyme, obtained after digestion with clostripain, possessed broad spectrum antimicrobial action in vitro. This internal peptide is part of a helix-loop-helix domain (87-114 sequence of hen lysozyme) located at the upper lip of the active site cleft of lysozyme. The helix-loophelix (HLH) structures are known motifs commonly found in membrane-active and DNA-binding proteins. To evaluate the contribution of the HLH peptide to the antimicrobial properties of lysozyme, the HLH sequence and its secondary structure derivatives of chicken and human lysozyme were synthesized and tested for antimicrobial activity against several bacterial strains. We found that the full HLH peptide of both chicken and human lysozymes was potently microbicidal against both Gram-positive and Gram-negative bacteria and the fungus Candida albicans. The N-terminal helix of HLH was specifically bactericidal to Gram-positive bacteria, whereas the C-terminal helix was bactericidal to all tested strains. Outer and inner membrane permeabilization studies, as well as measurements of transmembrane electrochemical potentials, provided evidence that HLH peptide and its C-terminal helix domain kill Gram-negative bacteria by crossing the outer membrane via self-promoted uptake and causing damage to the inner membrane through channel formation. The results are discussed in terms of proposed mechanisms for the catalytically independent antimicrobial activity of lysozyme that offer a new strategy for the design of potential antimicrobial drugs in the treatment of infectious diseases.

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Lysozyme interactions with phospholipid vesicles: relationships with fusion and release of aqueous content

Cited by 49 publications

References 18 publications

Modulation of physiological and pathological activities of lysozyme by biological membranes

Modulation of physiological and pathological activities of lysozyme by biological membranes

Penetration and Saturation of Lysozyme in Phospholipid Bilayers

A Helix-Loop-Helix Peptide at the Upper Lip of the Active Site Cleft of Lysozyme Confers Potent Antimicrobial Activity with Membrane Permeabilization Action

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