Fusogenic properties of the Ectodomain of HCV E2 envelope protein.
Biochim Biophys Acta Biomembr
; 1860(3): 728-736, 2018 Mar.
Article
en En
| MEDLINE
| ID: mdl-29273334
ABSTRACT
The steps leading from hepatitis C virus (HCV) attachment to the hepatocytes to the fusion of viral and cellular membranes remain uncharacterized. In this regard, we have studied the mechanism underlying the HCV fusion process using liposomes and a truncated form of E2 protein lacking the transmembrane region, E2661 (amino acids 384-661). E2661 has been previously obtained by using the baculovirus expression system and shown to behave as an independent folding domain (M. Rodriguez-Rodriguez, D. Tello, B. Yelamos, J. Gomez-Gutierrez, B. Pacheco, S. Ortega, A.G. Serrano, D.L. Peterson, F. Gavilanes, Structural properties of the ectodomain of hepatitis C virus E2 envelope protein, Virus Res. 139 (2009) 91-99). This form has been used in lipid-protein interaction studies with different model vesicles, at different pHs and by employing a variety of fluorescent assays. The obtained results indicate that E2661 induces vesicle aggregation, lipid mixing and liposome leakage, reaching higher values in the presence of negatively charged phospholipids and cholesterol at acidic pH. Therefore, the results of these studies would be indicative of an HCV infection process through receptor mediated endocytosis. Accordingly, E2 might be important in the HCV initial infective steps, interacting with the target membranes and giving rise to their subsequent destabilization.
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Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Proteínas del Envoltorio Viral
/
Hepacivirus
/
Internalización del Virus
Idioma:
En
Revista:
Biochim Biophys Acta Biomembr
Año:
2018
Tipo del documento:
Article
País de afiliación:
España