Full-length CD4 electroinserted in the erythrocyte membrane as a long-lived inhibitor of infection by human immunodeficiency virus.

Zeira, Michael; Tosi, Pierre-François; Mouneimne, Youssef; Lazarte, J. E.; Sneed, Loyd; Volsky, David J.; Nicolau, Claude

doi:10.1073/pnas.88.10.4409

Cited by 63 publications

(26 citation statements)

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“…As another example, one can mention electro-insertion of proteins into cell membranes. 55 Depending on the type of biomembranes and proteins targeted for insertion, different scenarios can be realized. In particular, the electric-field-induced insertion of proteins can be accompanied by electroporation.…”

Section: Discussionmentioning

confidence: 99%

Electroporation of Asymmetric Phospholipid Membranes

Gurtovenko

Lyulina

2014

J. Phys. Chem. B

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As plasma membranes of animal cells are known to be asymmetric, the transmembrane lipid asymmetry, being essential for many membranes' properties and functions, should be properly accounted for in model membrane systems. In this paper, we employ atomic-scale molecular dynamics simulations to explore electroporation phenomena in asymmetric model membranes comprised of phosphatidylcholine (PC) and phosphatidylethanolamine (PE) lipid monolayers that mimic the outer and inner leaflets of plasma membranes, respectively. Our findings clearly demonstrate that the molecular mechanism of electroporation in asymmetric phospholipid membranes differs considerably from the picture observed for their single-component symmetric counterparts: The initial stages of electric-field-induced formation of a water-filled pore turn out to be asymmetric and occur mainly on the PC side of the PC/PE membrane. In particular, water molecules penetrate in the membrane interior mostly from the PC side, and the reorientation of lipid head groups, being crucial for stabilizing the hydrophilic pore, also takes place in the PC leaflet. In contrast, the PE lipid head groups do not enter the central region of the membrane until the water pore becomes rather large and partly stabilized by PC head groups. Such behavior implies that the PE leaflet is considerably more robust against an electric field most likely due to interlipid hydrogen bonding. We also show that an electric field induces asymmetric changes in the lateral pressure profile of PC/PE membranes, decreasing the cohesion between lipid molecules predominantly in the PC membrane leaflet. Overall, our simulations provide compelling evidence that the transmembrane lipid asymmetry can be essential for understanding electroporation phenomena in living cells.

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Section: Discussionmentioning

confidence: 99%

Electroporation of Asymmetric Phospholipid Membranes

Gurtovenko

Lyulina

2014

J. Phys. Chem. B

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“…Recent studies reported the so-called 'electroin-sertion' of proteins, having a membrane-spanning sequence, into mouse red blood cell or Chinese hamster ovary cell membrane by exposing the cell suspension to electrical field pulses (Mouneimne et al, 1989(Mouneimne et al, , 1990Zeira et al, 1991 ;El Ouagari et al, 1993). This stable association (lifetime greater than several days) suggests that a transmembrane location of the protein was present.…”

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confidence: 99%

Electropermeabilization mediates a stable insertion of glycophorin A with Chinese hamster ovary cell membranes

Ouagari

Benoist

Sixou

et al. 1994

European Journal of Biochemistry

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Electropulsation allowed us to incorporate glycophorin A, an integral membrane protein, into mammalian nucleated cell membranes (Chinese hamster ovary cells). The induction of stable protein association is effective only when the field intensity is higher than its threshold value, creating membrane permeabilization to small molecules. Under controlled conditions, cell viability was only slightly altered by this treatment. Pulse number and duration controlled both the number of modified cells and incorporated molecules. The phenomena was temperature dependent. An average of 5 X104 moleculeskell was bound. About 80% of cells in the pulsed population were observed to incorporate glycophorin. The protein incorporation was shown to be stable 48 h after electroassociation. Electrically bound proteins were shared between the cells after each division. As enhanced binding is detected if glycophorin is added after the pulses, it is the long-lived alteration of the membrane mediated by the pulses which supports the association.It is commonly accepted that the driving force for the spontaneous incorporation of proteins is hydrophobic effect. However, a number of other effects may support or counteract this hydrophobic effect. Generally, the free energy of protein incorporation includes four contributions which arise from a change of water structure, protein state, lipid state, bonds between protein and water or lipid molecules. Nevertheless, the central questions of how hydrophobic sequences would be transferred from an aqueous to an hydrophobic environment and how the polar regions of protein that span the membrane would be transferred across the hydrocarbon core of the bilayer, have not been emphasized. So, this makes it exceedingly unlikely that insertion of integral protein occurs directly across the lipid bilayer (Singer, 1990;Singer and Yaffe, 1990; Singer et al., 1987a, b). The membrane contribution, which has been neglected until now, necessarily appears important allowing the penetration of macromolecules with strongly polar segments. Thermodynamics of protein insertion in lipid systems imply the occurrence of the lipid matrix perturbation. Thus, protein incorporation thermodynamics ( J i m and Zakim, 1987;Jahnig, 1983) show a favourable contribution of electrostatic forces and hydrophobic forces which occur on the membrane-spanning sequence, whereas hydration forces (Pargesian and Rau, 1984) and hydrophobic forces which occur on the protein polar segments prevent incorporation. Spontaneous insertion takes place if the first component is stronger than the second one. Such a case would occur only if the membrane is in an 'excited' state.Electropulsation can create such an 'excited' state of the membrane. Recent studies reported the so-called 'electroinCorrespondence to J. Teissie,

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“…Studies have reported the so-called "electroinsertion" of proteins, having a membrane spanning sequence, such as glycophorin and CD4, into eukaryotic cell membranes by exposing the cell suspension to electric field pulses (23)(24)(25)(26)(27)(28)(29). No spontaneous insertion of glycophorin was observed without the electrical treatment.…”

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confidence: 99%