Interaction of Staphylococcus aureus .delta.-lysin with phospholipid monolayers

Bhakoo, Manmohan; Birkbeck, T. H.; Freer, John H.

doi:10.1021/bi00269a039

Cited by 50 publications

(33 citation statements)

References 18 publications

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“…The same results were obtained with some cardiotoxins from Naja mossambica mossambica [29]. On the other hand, 6 lysin, in which the positive charges are less localized [30], does not show any specificity for different phospholipids. The phosphatidylcholine transfer protein has a very strong affinity for acidic liposomes [31].…”

Section: Interaction Of H D L With Negatively Charged Vesicles Is Regsupporting

confidence: 80%

The influence of the internal content of negatively charged liposomes on their interaction with high‐density lipoprotein

Vidal

Bienvenüe

Sainte‐Marie

et al. 1984

European Journal of Biochemistry

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The release of the internal content of negatively charged phosphatidylcholine/phosphatidylserine vesicles under the influence of high density lipoprotein was studied. Under standard conditions (the same composition outside and inside the compartment) the leakage of negative liposomes increased significantly. However, a high internal concentration of calcein provoked a sealing effect, exhibited both in sucrose and in calcein release. This sealing effect is not related to the size of vesicles, the fluidity of the membrane, the distribution of phosphatidylserine molecules, or the membrane potential. Our data indicate that surface potential influences this effect, probably in addition to a lateral pressure effect such as with cholesterol. The surface potential, as measured by the water-lipid partition coefficient of fatty acids, is strongly affected by internal ionic strength when liposomes contain calcein as well as other polyanions (6-carboxyfluorescein, sodium citrate).The liposome-mediated transfer of drugs to cells is currently the object of many investigations (see [l] for a review). Numerous factors are crucial to the transfer: the encapsulation ratio, the stability of vesicles in serum, the overall clearance rate, the specificity of the interaction and the internalization yield of vesicles. The influence of many of these different factors has been analyzed, viz. size, charges, or composition of vesicles. Several generally accepted rules appear to be applied by most authors. For instance, negatively charged vesicles in a liquid crystal state are often used. Cholesterol is generally added in order to restrain the HDL-provoked leakage of the internal content of the liposomes. With this procedure, a weak internalization yield is obtained, even in uitro where poly(ethy1ene glycol) can be added to increase the fusion process [2].The role of HDL particles in the disruption of PtdCho vesicles is now well documented [3], but almost nothing is known about HDL-negatively charged vesicles interactions. In order to assess the use of this kind of liposome in uivo, we investigated its interaction with serum lipoproteins. This paper is devoted to the influence of the internal content of negative vesicles on their interaction with HDL particles. We show that high internal ionic strength decreases the vesicles surface potential. This leads to a very strong attenuation of HDLvesicle interaction, corresponding to a sealing effect analogous to the one observed with cholesterol.

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Section: Interaction Of H D L With Negatively Charged Vesicles Is Regsupporting

confidence: 80%

The influence of the internal content of negatively charged liposomes on their interaction with high‐density lipoprotein

Vidal

Bienvenüe

Sainte‐Marie

et al. 1984

European Journal of Biochemistry

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“…Dempsey, 1990). Although it has a higher affinity for negatively charged phospholipids (Bhakoo et al, 1982;Batenburg et al, 1988), melittin is equally efficient in lysing erythrocytes (Sessa et al, 1969) or bacteria (Boman et al, 1989). This is in marked contrast to PGLa or magainin which do not show any significant interaction with choline phosphatides, the main phospholipids of erythrocytes.…”

Section: Discussionmentioning

confidence: 99%

Structural Aspects of the Interaction of peptidyl‐glycylleucine‐carboxyamide, a Highly Potent Antimicrobial Peptide from Frog Skin, with Lipids

Latal

Degovics

Epand

et al. 1997

European Journal of Biochemistry

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The interaction of PGLa (peptidyl-glycylleucine-carboxyamide), a 21 -amino-acid residue cationic peptide, isolated from the skin of the South African clawed frog, Xenopus luevis, with model membrane systems was investigated. Our studies focussed on the importance of the difference in the phospholipid composition of bacterial and erythrocyte membranes. This is of particular interest to gain information on the specificity of membranolysis exhibited by this peptide against bacteria but not against erythrocytes.In phosphate buffer at physiological pH, as well as in the presence of the zwitterionic phosphatidylcholine and sphingomyelin, the peptide had a random structure but it adopted an a-helical conformation in the presence of negatively charged lipids. Furthermore, calorimetric experiments showed that PGLa had no effects on the thermotropic phase behavior of liposomes composed of the choline phosphatides, while separation of a distinct peptide-rich domain was observed for phosphatidylglycerol liposomes. In addition to the main transition of pure 1,2-dipalmitoylglycerophosphoglycerol at 40°C a second transition owing to the peptide-perturbed lipid domains was found at 41 "C. This conclusion is supported by X-ray diffraction experiments which indicated that PGLa penetrates into the hydrophobic core of the bilayer inducing an untilting of the hydrocarbon chains as observed in the gel phase of the pure lipid. These results demonstrate that this antibacterial peptide specifically interacts with negatively charged lipid membranes, which are characteristic of bacterial membranes. This can be explained based on the structural features of PGLa.

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“…Correspondence: A.M. Batenburg concentrated at the C-terminus, its structure is amphiphilic and makes it interact with detergents and natural and artifical pure lipid membranes [1][2][3][4][5]. Melittin influences the permeability properties of membranes [6][7][8][9][10] and affects the activity of membrane bound enzymes [11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Melittin induces HII phase formation in cardiolipin model membranes

Batenburg

Hibbeln

Verkleij

et al. 1987

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The interaction of melittin with bovine heart cardiolipin model membranes was investigated via binding assays, 3t P-NMR, freeze-fracture electron microscopy, small angle X-ray diffraction and fluorescence based fusion assays. A strong binding (K d < 10-7 M) appeared to be accompanied by the formation of large structures, resulting from a fusion process of extremely fast initial rate. As the melittin content is increased, bilayer structure is gradually lost and from a cardiolipin to melittin ratio of about 6 the lipid starts to organize itself in an hexagonal H ii phase. At lower temperatures (T < 40 ° C) the coexistence of another structure is observed, characterized by a broad isotropic 31p-NMR signal and giving rise to sharp X-ray reflections, most probably a cubic phase, as suggested also by freeze-fracture images, showing orderly stacked particles. The results are discussed in relation to contrasting observations on the structural changes induced by melittin in the zwitterionic phospholipid system of dipalmitoylphosphatidylcholine (Dufourcq, J. et al. (1986) Biochim. Biophys. Acta 859, 33-48). The biological relevance of the observations with respect to the process of protein insertion into membranes is indicated.

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Interaction of Staphylococcus aureus .delta.-lysin with phospholipid monolayers

Cited by 50 publications

References 18 publications

The influence of the internal content of negatively charged liposomes on their interaction with high‐density lipoprotein

The influence of the internal content of negatively charged liposomes on their interaction with high‐density lipoprotein

Structural Aspects of the Interaction of peptidyl‐glycylleucine‐carboxyamide, a Highly Potent Antimicrobial Peptide from Frog Skin, with Lipids

Melittin induces HII phase formation in cardiolipin model membranes

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