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 Hepatitis C Virus Is Primed by CD81 Protein for Low pH-dependent Fusion

2011 ◽  
Vol 286 (35) ◽  
pp. 30361-30376 ◽  
Author(s):  
Nishi R. Sharma ◽  
Guaniri Mateu ◽  
Marlene Dreux ◽  
Arash Grakoui ◽  
François-Loïc Cosset ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Low Ph ◽  
Ph Dependent

Inactivation of Hepatitis C Virus in Low pH Intravenous Immunoglobulin

Biologicals ◽  
1994 ◽  
Vol 22 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Robert E. Louie ◽  
Cynthia J. Galloway ◽  
Michael L. Dumas ◽  
Melvin F. Wong ◽  
G. Mitra
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Intravenous Immunoglobulin ◽  
Low Ph

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

scholarly journals The Baculovirus GP64 Protein Mediates Highly Stable Infectivity of a Human Respiratory Syncytial Virus Lacking Its Homologous Transmembrane Glycoproteins

2004 ◽  
Vol 78 (1) ◽  
pp. 124-135 ◽  
Author(s):  
A. G. P. Oomens ◽  
Gail W. Wertz
Keyword(s):  
Respiratory Syncytial Virus ◽  
Membrane Fusion ◽  
Mammalian Cells ◽  
Chimeric Protein ◽  
Low Ph ◽  
Human Respiratory Syncytial Virus ◽  
Dependent Manner ◽  
Practical Applications ◽  
Ph Dependent ◽  
Syncytial Virus

ABSTRACT Baculovirus GP64 is a low-pH-dependent membrane fusion protein required for virus entry and cell-to-cell transmission. Recently, GP64 has generated interest for practical applications in mammalian systems. Here we examined the membrane fusion function of GP64 from Autographa californica multiple nucleopolyhedrovirus (AcMNPV) expressed in mammalian cells, as well as its capacity to functionally complement a mammalian virus, human respiratory syncytial virus (HRSV). Both authentic GP64 and GP64/F, a chimeric protein in which the GP64 cytoplasmic tail domain was replaced with the 12 C-terminal amino acids of the HRSV fusion (F) protein, induced low-pH-dependent cell-cell fusion when expressed transiently in HEp-2 (human) cells. Levels of surface expression and syncytium formation were substantially higher at 33°C than at 37°C. The open reading frames (ORFs) encoding GP64 or GP64/F, along with two marker ORFs encoding green fluorescent protein (GFP) and β-glucuronidase (GUS), were used to replace all three homologous transmembrane glycoprotein ORFs (small hydrophobic SH, attachment G, and F) in a cDNA of HRSV. Infectious viruses were recovered that lacked the HRSV SH, G, and F proteins and expressed instead the GP64 or GP64/F protein and the two marker proteins GFP and GUS. The properties of these viruses, designated RSΔsh,g,f/GP64 or RSΔsh,g,f/GP64/F, respectively, were compared to a previously described HRSV expressing GFP in place of SH but still containing the wild-type HRSV G and F proteins (RSΔsh [A. G. Oomens, A. G. Megaw, and G. W. Wertz, J. Virol., 77:3785-3798, 2003]). By immunoelectron microscopy, the GP64 and GP64/F proteins were shown to incorporate into HRSV-induced filaments at the cell surface. Antibody neutralization, ammonium chloride inhibition, and replication levels in cell culture showed that both GP64 proteins efficiently mediated infectivity of the respective viruses in a temperature-sensitive, low-pH-dependent manner. Furthermore, RSΔsh,g,f/GP64 and RSΔsh,g,f/GP64/F replicated to higher levels and had significantly higher stability of infectivity than HRSVs containing the homologous HRSV G and F proteins. Thus, GP64 and a GP64/HRSV F chimeric protein were functional and efficiently complemented an unrelated human virus in mammalian cells, producing stable, infectious virus stocks. These results demonstrate the potential of GP64 for both practical applications requiring stable pseudotypes in mammalian systems and for studies of viral glycoprotein requirements in assembly and pathogenesis.

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
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