Characterization of a putative fusogenic sequence in the E2 hepatitis G virus protein.
With 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.
Larios
Cristina
C
Department of Peptide and Protein Chemistry, IIQAB-CSIC, Jordi Girona, Salgado 18-26, 08034 Barcelona, Spain.
Casas
Jordi
J
Alsina
María A
MA
Mestres
Concepción
C
Gómara
María J
MJ
Haro
Isabel
I
D002942:Circular Dichroism / Q000379:methods; D029407:GB virus C / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008567:Membranes, Artificial; D008956:Models, Chemical; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000378:metabolism
D008051:Lipid Bilayers; D008567:Membranes, Artificial; D014759:Viral Envelope Proteins; C107619:glycoprotein E2, GB virus C