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Membrane-perturbing properties of three peptides corresponding to the ectodomain of hepatitis C virus E2 envelope protein

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Pacheco, Beatriz and Gómez-Gutiérrez, Julián and Yélamos, Belén and Delgado, Carmen and Roncal, Fernando and Albar, Juan P. and Peterson, Darrell and Gavilanes, Francisco (2006) Membrane-perturbing properties of three peptides corresponding to the ectodomain of hepatitis C virus E2 envelope protein. Biochimica et Biophysica Acta - Biomembranes, 1758 (6). pp. 755-763. ISSN 0005-2736

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Official URL: http://www.sciencedirect.com/science/article/pii/S0005273606001714



Abstract

Based on the predicted capacity to interact with membranes at the interface, we have found three regions in the ectodomain of the hepatitis C virus envelope glycoprotein E2 (430-449, 543-560 and 603-624) with the ability to destabilize membranes. Three peptides corresponding to the sequence of these regions have been synthesized and their interaction with liposomes have been characterized. The three peptides were able to insert deeply into the hydrophobic core of negatively charged phospholipids as stated by fluorescence depolarization of the probe 1,6-diphenyl-1,3,5- hexatriene. Peptides E2430-449 and E2603-624 were able to induce aggregation of phosphatidylglycerol vesicles in a concentration-dependent manner both at neutral and acidic pH while peptide E2543-560 did not induce any increase of optical density at 360 nm in the concentration range studied. The three peptides induced lipid mixing and the release of the internal contents in a dose-dependent manner when acidic phospholipids were used. Fourier transformed infrared spectroscopy indicated that the peptides adopted mainly a β-sheet conformation which is not modified by the presence of acidic phospholipids. Taken together, our results point out to the involvement of these three regions in the fusion mechanism of HCV at the plasma membrane level.


Item Type:Article
Uncontrolled Keywords:TRANSFORM INFRARED-SPECTROSCOPY; 2 FUSION PEPTIDES; VIRAL FUSION; CELL-FUSION; GLYCOPROTEIN; MODEL; PH; DESTABILIZATION; SEQUENCES; RECEPTOR
Subjects:Sciences > Chemistry > Biochemistry
ID Code:33614
Deposited On:16 Oct 2015 08:04
Last Modified:16 Oct 2015 08:04

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