Scavenger Receptor BI and BII Expression Levels Modulate Hepatitis C Virus Infectivity

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Scavenger Receptor BI and BII Expression Levels Modulate Hepatitis C Virus Infectivity. / Grove, Joseph; Huby, T; Stamataki, Zacharenia; Vanwolleghem, T; Meuleman, P; Farquhar, Michelle; Schwarz, A; Moreau, M; Owen, JS; Leroux-Roels, G; Balfe, Peter; McKeating, Jane.

In: Journal of virology, Vol. 81, No. 7, 24.01.2007, p. 3162-9.

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Grove, Joseph ; Huby, T ; Stamataki, Zacharenia ; Vanwolleghem, T ; Meuleman, P ; Farquhar, Michelle ; Schwarz, A ; Moreau, M ; Owen, JS ; Leroux-Roels, G ; Balfe, Peter ; McKeating, Jane. / Scavenger Receptor BI and BII Expression Levels Modulate Hepatitis C Virus Infectivity. In: Journal of virology. 2007 ; Vol. 81, No. 7. pp. 3162-9.

Bibtex

@article{3a557c9792744f3180988257cf1b85b3,
title = "Scavenger Receptor BI and BII Expression Levels Modulate Hepatitis C Virus Infectivity",
abstract = "Hepatitis C virus (HCV) enters cells via a pH- and clathrin-dependent endocytic pathway. Scavenger receptor BI (SR-BI) and CD81 are important entry factors for HCV internalization into target cells. The SR-BI gene gives rise to at least two mRNA splice variants, SR-BI and SR-BII, which differ in their C termini. SR-BI internalization remains poorly understood, but SR-BII is reported to endocytose via a clathrin-dependent pathway, making it an attractive target for HCV internalization. We demonstrate that HCV soluble E2 can interact with human SR-BI and SR-BII. Increased expression of SR-BI and SR-BII in the Huh-7.5 hepatoma cell line enhanced HCV strain J6/JFH and JFH infectivity, suggesting that endogenous levels of these receptors limit infection. Elevated expression of SR-BI, but not SR-BII, increased the rate of J6/JFH infection, which may reflect altered intracellular trafficking of the splice variants. In human plasma, HCV particles have been reported to be complexed with lipoproteins, suggesting an indirect interaction of the virus with SR-BI and other lipoprotein receptors. Plasma from J6/JFH-infected uPA-SCID mice transplanted with human hepatocytes demonstrates an increased infectivity for SR-BI/II-overexpressing Huh-7.5 cells. Plasma-derived J6/JFH infectivity was inhibited by an anti-E2 monoclonal antibody, suggesting that plasma virus interaction with SR-BI was glycoprotein dependent. Finally, anti-SR-BI antibodies inhibited the infectivity of cell culture- and plasma-derived J6/JFH, suggesting a critical role for SR-BI/II in HCV infection.",
author = "Joseph Grove and T Huby and Zacharenia Stamataki and T Vanwolleghem and P Meuleman and Michelle Farquhar and A Schwarz and M Moreau and JS Owen and G Leroux-Roels and Peter Balfe and Jane McKeating",
year = "2007",
month = jan,
day = "24",
doi = "10.1128/JVI.02356-06",
language = "English",
volume = "81",
pages = "3162--9",
journal = "Journal of virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "7",

}

RIS

TY - JOUR

T1 - Scavenger Receptor BI and BII Expression Levels Modulate Hepatitis C Virus Infectivity

AU - Grove, Joseph

AU - Huby, T

AU - Stamataki, Zacharenia

AU - Vanwolleghem, T

AU - Meuleman, P

AU - Farquhar, Michelle

AU - Schwarz, A

AU - Moreau, M

AU - Owen, JS

AU - Leroux-Roels, G

AU - Balfe, Peter

AU - McKeating, Jane

PY - 2007/1/24

Y1 - 2007/1/24

N2 - Hepatitis C virus (HCV) enters cells via a pH- and clathrin-dependent endocytic pathway. Scavenger receptor BI (SR-BI) and CD81 are important entry factors for HCV internalization into target cells. The SR-BI gene gives rise to at least two mRNA splice variants, SR-BI and SR-BII, which differ in their C termini. SR-BI internalization remains poorly understood, but SR-BII is reported to endocytose via a clathrin-dependent pathway, making it an attractive target for HCV internalization. We demonstrate that HCV soluble E2 can interact with human SR-BI and SR-BII. Increased expression of SR-BI and SR-BII in the Huh-7.5 hepatoma cell line enhanced HCV strain J6/JFH and JFH infectivity, suggesting that endogenous levels of these receptors limit infection. Elevated expression of SR-BI, but not SR-BII, increased the rate of J6/JFH infection, which may reflect altered intracellular trafficking of the splice variants. In human plasma, HCV particles have been reported to be complexed with lipoproteins, suggesting an indirect interaction of the virus with SR-BI and other lipoprotein receptors. Plasma from J6/JFH-infected uPA-SCID mice transplanted with human hepatocytes demonstrates an increased infectivity for SR-BI/II-overexpressing Huh-7.5 cells. Plasma-derived J6/JFH infectivity was inhibited by an anti-E2 monoclonal antibody, suggesting that plasma virus interaction with SR-BI was glycoprotein dependent. Finally, anti-SR-BI antibodies inhibited the infectivity of cell culture- and plasma-derived J6/JFH, suggesting a critical role for SR-BI/II in HCV infection.

AB - Hepatitis C virus (HCV) enters cells via a pH- and clathrin-dependent endocytic pathway. Scavenger receptor BI (SR-BI) and CD81 are important entry factors for HCV internalization into target cells. The SR-BI gene gives rise to at least two mRNA splice variants, SR-BI and SR-BII, which differ in their C termini. SR-BI internalization remains poorly understood, but SR-BII is reported to endocytose via a clathrin-dependent pathway, making it an attractive target for HCV internalization. We demonstrate that HCV soluble E2 can interact with human SR-BI and SR-BII. Increased expression of SR-BI and SR-BII in the Huh-7.5 hepatoma cell line enhanced HCV strain J6/JFH and JFH infectivity, suggesting that endogenous levels of these receptors limit infection. Elevated expression of SR-BI, but not SR-BII, increased the rate of J6/JFH infection, which may reflect altered intracellular trafficking of the splice variants. In human plasma, HCV particles have been reported to be complexed with lipoproteins, suggesting an indirect interaction of the virus with SR-BI and other lipoprotein receptors. Plasma from J6/JFH-infected uPA-SCID mice transplanted with human hepatocytes demonstrates an increased infectivity for SR-BI/II-overexpressing Huh-7.5 cells. Plasma-derived J6/JFH infectivity was inhibited by an anti-E2 monoclonal antibody, suggesting that plasma virus interaction with SR-BI was glycoprotein dependent. Finally, anti-SR-BI antibodies inhibited the infectivity of cell culture- and plasma-derived J6/JFH, suggesting a critical role for SR-BI/II in HCV infection.

U2 - 10.1128/JVI.02356-06

DO - 10.1128/JVI.02356-06

M3 - Article

C2 - 17215280

VL - 81

SP - 3162

EP - 3169

JO - Journal of virology

JF - Journal of virology

SN - 0022-538X

IS - 7

ER -