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Characterization of a putative fusogenic sequence in the E2 hepatitis G virus protein

AutorLarios, Cristina; Casas, Jordi; Alsina, M. Asunción; Mestres, Concepció; Gómara Elena, María José; Haro Villar, Isabel
Palabras claveHepatitis G virus
E2 structural protein
Fusogenic peptide
Solid-phase peptide synthesis
Model membranes
Fluorescence spectroscopy
Differential scanning calorimetry
Circular dichroism
Fourier-transform infrared spectroscopy
Fecha de publicación1-ago-2005
CitaciónArchives of Biochemistry and Biophysics 442(2): 149-159 (2005)
ResumenWith the aim of better understanding the fusion process mediated by the envelope proteins of the hepatitis G virus (HGV/GBV-C), we have investigated the interaction with model membranes of two overlapping peptides [(267–284) and (279–298)] belonging to the E2 structural protein. The peptides were compared for their ability to perturb lipid bilayers by means of different techniques such as differential scanning calorimetry and fluorescence spectroscopy. Furthermore, the conformational behaviour of the peptides in different membrane environments was studied by Fourier-transform infrared spectroscopy and circular dichroism. The results showed that only the E2(279–298) peptide sequence was able to bind with high affinity to negatively charged membranes, to permeabilize efficiently negative lipid bilayers, to induce haemolysis, and to promote inter-vesicle fusion. This fusogenic activity could be related to the induced peptide conformation upon interaction with the target membrane.
Descripción11 pages, 8 figures, 2 tables.-- PMID: 16165082 [PubMed].-- Printed version published Oct 15, 2005.
Supporting information available at: http://dx.doi.org/10.1016/j.abb.2005.06.027
Versión del editorhttp://dx.doi.org/10.1016/j.abb.2005.06.027
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