scholarly journals The Exchangeable Apolipoprotein ApoC-I Promotes Membrane Fusion of Hepatitis C Virus

2007 ◽  
Vol 282 (44) ◽  
pp. 32357-32369 ◽  
Author(s):  
Marlène Dreux ◽  
Bertrand Boson ◽  
Sylvie Ricard-Blum ◽  
Jennifer Molle ◽  
Dimitri Lavillette ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Membrane Fusion ◽  
Exchangeable Apolipoprotein

scholarly journals Hepatitis C Virus Glycoproteins Mediate Low pH-dependent Membrane Fusion with Liposomes

2006 ◽  
Vol 281 (7) ◽  
pp. 3909-3917 ◽  
Author(s):  
Dimitri Lavillette ◽  
Birke Bartosch ◽  
Delphine Nourrisson ◽  
Géraldine Verney ◽  
François-Loïc Cosset ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Membrane Fusion ◽  
Low Ph ◽  
Ph Dependent

scholarly journals A central hydrophobic E1 region controls the pH range of hepatitis C virus membrane fusion and susceptibility to fusion inhibitors

2019 ◽  
Vol 70 (6) ◽  
pp. 1082-1092 ◽  
Author(s):  
Dominic H. Banda ◽  
Paula M. Perin ◽  
Richard J.P. Brown ◽  
Daniel Todt ◽  
Wladimir Solodenko ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Membrane Fusion ◽  
Fusion Inhibitors ◽  
Ph Range

Neutralizing Host Responses in Hepatitis C Virus Infection Target Viral Entry at Postbinding Steps and Membrane Fusion

2008 ◽  
Vol 135 (5) ◽  
pp. 1719-1728.e1 ◽  
Author(s):  
Anita Haberstroh ◽  
Eva K. Schnober ◽  
Mirjam B. Zeisel ◽  
Patric Carolla ◽  
Heidi Barth ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Virus Infection ◽  
Membrane Fusion ◽  
Viral Entry ◽  
Host Responses ◽  
Hepatitis C Virus Infection

Stapled peptide-based membrane fusion inhibitors of hepatitis C virus

2013 ◽  
Vol 21 (12) ◽  
pp. 3547-3554 ◽  
Author(s):  
Hong-Kui Cui ◽  
Jie Qing ◽  
Ye Guo ◽  
Yu-Jia Wang ◽  
Li-Jia Cui ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Membrane Fusion ◽  
Stapled Peptide ◽  
Fusion Inhibitors

607 NEUTRALIZING HOST RESPONSES IN HEPATITIS C VIRUS INFECTION TARGET VIRAL ENTRY AT POST-BINDING STEPS AND MEMBRANE FUSION

2008 ◽  
Vol 48 ◽  
pp. S226
Author(s):  
A. Haberstroh ◽  
E.K. Schnober ◽  
P. Carolla ◽  
M.B. Zeisel ◽  
H. Barth ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Virus Infection ◽  
Membrane Fusion ◽  
Viral Entry ◽  
Host Responses ◽  
Hepatitis C Virus Infection

scholarly journals Characterization of hepatitis C virus pseudoparticles by cryo-transmission electron microscopy using functionalized magnetic nanobeads

2010 ◽  
Vol 91 (8) ◽  
pp. 1919-1930 ◽  
Author(s):  
Pierre Bonnafous ◽  
Marie Perrault ◽  
Olivier Le Bihan ◽  
Birke Bartosch ◽  
Dimitri Lavillette ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Membrane Fusion ◽  
Magnetic Beads ◽  
Neutral Ph ◽  
Transmission Electron ◽  
Magnetic Nanobeads

Cell entry and membrane fusion of the hepatitis C virus (HCV) depend on its envelope glycoproteins E1 and E2. HCV pseudotyped particles (HCVpps) are relevant and popular models to study the early steps of the HCV life cycle. However, no structural characterization of HCVpp has been available so far. Using cryo-transmission electron microscopy (cryo-TEM), providing structural information at nanometric resolution, the molecular details of HCVpps and their fusion with liposomes were studied. Cryo-TEM revealed HCVpps as regular 100 nm spherical structures containing the dense retroviral nucleocapsid surrounded by a lipid bilayer. E1–E2 glycoproteins were not readily visible on the membrane surface. Pseudoparticles bearing the E1–E2 glycoproteins of Semliki forest virus looked similar, whereas avian influenza A virus (fowl plague virus) haemagglutinin/neuraminidase-pseudotyped particles exhibited surface spikes. To further characterize HCVpp structurally, a novel method was designed based on magnetic beads covered with anti-HCV antibodies to enrich the samples with particles containing E1–E2. This strategy efficiently sorted HCVpps, which were then directly observed by cryo-TEM in the presence or absence of liposomes at low or neutral pH. After acidification, HCVpps looked the same as at neutral pH and closely contacted the liposomes. These are the first visualizations of early HCV membrane fusion events at the nanometer scale. Furthermore, fluorimetry analysis revealed a relative resistance of HCVpps regarding their fusion capacity when exposed to low pH. This study therefore brings several new molecular details to HCVpp characterization and this efficient strategy of virion immunosorting with magnetic nanobeads is direct, efficient and adaptable to extensive characterization of any virus at a nanometric resolution.

scholarly journals Aloperine inhibits hepatitis C virus entry into cells by disturbing internalisation from endocytosis to the membrane fusion process

2020 ◽  
Vol 883 ◽  
pp. 173323 ◽  
Author(s):  
Xiao-Qin Lv ◽  
Li-Li Zou ◽  
Jia-Li Tan ◽  
Hu Li ◽  
Jian-Rui Li ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Membrane Fusion ◽  
Virus Entry ◽  
Fusion Process

scholarly journals Fluoxazolevir inhibits hepatitis C virus infection in humanized chimeric mice by blocking viral membrane fusion

2020 ◽  
Vol 5 (12) ◽  
pp. 1532-1541
Author(s):  
Christopher D. Ma ◽  
Michio Imamura ◽  
Daniel C. Talley ◽  
Adam Rolt ◽  
Xin Xu ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Virus Infection ◽  
Membrane Fusion ◽  
Hepatitis C Virus Infection ◽  
Chimeric Mice ◽  
Viral Membrane ◽  
Viral Membrane Fusion
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