Hepatitis C virus entry depends on clathrin-mediated endocytosis.
Identifieur interne : 000109 ( Hal/Curation ); précédent : 000108; suivant : 000110Hepatitis C virus entry depends on clathrin-mediated endocytosis.
Auteurs : Emmanuelle Blanchard [France] ; Sandrine Belouzard [France] ; Lucie Goueslain [France] ; Takaji Wakita [Japon] ; Jean Dubuisson [France] ; Czeslaw Wychowski [France] ; Yves Rouillé [France]Source :
- Journal of Virology [ 0022-538X ] ; 2006-07-17.
Abstract
Due to difficulties in cell culture propagation, the mechanisms of hepatitis C virus (HCV) entry are poorly understood. Here, postbinding cellular mechanisms of HCV entry were studied using both retroviral particles pseudotyped with HCV envelope glycoproteins (HCVpp) and the HCV clone JFH-1 propagated in cell culture (HCVcc). HCVpp entry was measured by quantitative real-time PCR after 3 h of contact with target cells, and HCVcc infection was quantified by immunoblot analysis and immunofluorescence detection of HCV proteins expressed in infected cells. The functional role of clathrin-mediated endocytosis in HCV entry was assessed by small interfering RNA-mediated clathrin heavy chain depletion and with chlorpromazine, an inhibitor of clathrin-coated pit formation at the plasma membrane. In both conditions, HCVpp entry and HCVcc infection were inhibited. HCVcc infection was also inhibited by pretreating target cells with bafilomycin A1 or chloroquine, two drugs known to interfere with endosome acidification. These data indicate that HCV enters target cells by clathrin-mediated endocytosis, followed by a fusion step from within an acidic endosomal compartment.
Url:
DOI: 10.1128/JVI.00024-06
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<front><div type="abstract" xml:lang="en"> <p>Due to difficulties in cell culture propagation, the mechanisms of hepatitis C virus (HCV) entry are poorly understood. Here, postbinding cellular mechanisms of HCV entry were studied using both retroviral particles pseudotyped with HCV envelope glycoproteins (HCVpp) and the HCV clone JFH-1 propagated in cell culture (HCVcc). HCVpp entry was measured by quantitative real-time PCR after 3 h of contact with target cells, and HCVcc infection was quantified by immunoblot analysis and immunofluorescence detection of HCV proteins expressed in infected cells. The functional role of clathrin-mediated endocytosis in HCV entry was assessed by small interfering RNA-mediated clathrin heavy chain depletion and with chlorpromazine, an inhibitor of clathrin-coated pit formation at the plasma membrane. In both conditions, HCVpp entry and HCVcc infection were inhibited. HCVcc infection was also inhibited by pretreating target cells with bafilomycin A1 or chloroquine, two drugs known to interfere with endosome acidification. These data indicate that HCV enters target cells by clathrin-mediated endocytosis, followed by a fusion step from within an acidic endosomal compartment.</p>
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<hal api="V3"> <titleStmt> <title xml:lang="en">Hepatitis C virus entry depends on clathrin-mediated endocytosis.</title>
<author role="aut"> <persName> <forename type="first">Emmanuelle</forename>
<surname>Blanchard</surname>
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<idno type="halauthorid">136781</idno>
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<author role="aut"> <persName> <forename type="first">Sandrine</forename>
<surname>Belouzard</surname>
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<author role="aut"> <persName> <forename type="first">Lucie</forename>
<surname>Goueslain</surname>
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<idno type="halauthorid">136865</idno>
<affiliation ref="#struct-24511"></affiliation>
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<author role="aut"> <persName> <forename type="first">Takaji</forename>
<surname>Wakita</surname>
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<idno type="halauthorid">136863</idno>
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<author role="aut"> <persName> <forename type="first">Jean</forename>
<surname>Dubuisson</surname>
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<author role="aut"> <persName> <forename type="first">Czeslaw</forename>
<surname>Wychowski</surname>
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<author role="crp"> <persName> <forename type="first">Yves</forename>
<surname>Rouillé</surname>
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<editor role="depositor"> <persName> <forename>Jean</forename>
<surname>Dubuisson</surname>
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<funder>This work was supported by a grant from the “Agence Nationale de Recherche sur le Sida et les Hépatites Virales” (ANRS) to Y.R. and C.W.E.B. was supported by a postdoctoral fellowship from the ANRS. T.W. was partly supported by a grant from the Ministry of Health, Labor, and Welfare of Japan, the Program for Promotion of Fundamental Studies in Health Sciences of the National Institute of Biomedical Innovation (NIBIO), and Research on Health Sciences focusing on Drug Innovation from the Japan Health Sciences Foundation. J.D. is an international scholar of the Howard Hughes Medical Institute.</funder>
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<date type="whenModified">2019-10-15 16:06:25</date>
<date type="whenReleased">2006-10-11 12:38:27</date>
<date type="whenProduced">2006-07-17</date>
<ref type="externalLink" target="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1489042/pdf"></ref>
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<name key="113563"> <persName> <forename>Jean</forename>
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<idno type="halRefHtml">Journal of Virology, American Society for Microbiology, 2006, 80 (14), pp.6964-6972. ⟨10.1128/JVI.00024-06⟩</idno>
<idno type="halRef">Journal of Virology, American Society for Microbiology, 2006, 80 (14), pp.6964-6972. ⟨10.1128/JVI.00024-06⟩</idno>
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<idno type="stamp" n="RIIP_LILLE">Institut Pasteur de Lille</idno>
<idno type="stamp" n="RIIP">Institut Pasteur RIIP (Réseau International)</idno>
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<note type="popular" n="0">No</note>
<note type="peer" n="1">Yes</note>
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<sourceDesc> <biblStruct> <analytic> <title xml:lang="en">Hepatitis C virus entry depends on clathrin-mediated endocytosis.</title>
<author role="aut"> <persName> <forename type="first">Emmanuelle</forename>
<surname>Blanchard</surname>
</persName>
<idno type="halauthorid">136781</idno>
<affiliation ref="#struct-24511"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Sandrine</forename>
<surname>Belouzard</surname>
</persName>
<idno type="halauthorid">136792</idno>
<affiliation ref="#struct-24511"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Lucie</forename>
<surname>Goueslain</surname>
</persName>
<idno type="halauthorid">136865</idno>
<affiliation ref="#struct-24511"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Takaji</forename>
<surname>Wakita</surname>
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<idno type="halauthorid">136863</idno>
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<author role="aut"> <persName> <forename type="first">Jean</forename>
<surname>Dubuisson</surname>
</persName>
<idno type="halauthorid">136770</idno>
<affiliation ref="#struct-24511"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Czeslaw</forename>
<surname>Wychowski</surname>
</persName>
<idno type="halauthorid">136785</idno>
<affiliation ref="#struct-24511"></affiliation>
</author>
<author role="crp"> <persName> <forename type="first">Yves</forename>
<surname>Rouillé</surname>
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<email type="md5">fad0aed7670be7f6dc8c776dc12fbf29</email>
<email type="domain">ibl.fr</email>
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<idno type="issn">0022-538X</idno>
<idno type="eissn">1098-5514</idno>
<title level="j">Journal of Virology</title>
<imprint> <publisher>American Society for Microbiology</publisher>
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<biblScope unit="issue">14</biblScope>
<biblScope unit="pp">6964-6972</biblScope>
<date type="datePub">2006-07-17</date>
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<idno type="doi">10.1128/JVI.00024-06</idno>
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<textClass> <classCode scheme="mesh">Cell Line, Tumor</classCode>
<classCode scheme="mesh">Chlorpromazine/pharmacology</classCode>
<classCode scheme="mesh">Hepatitis C/metabolism*</classCode>
<classCode scheme="mesh">Humans</classCode>
<classCode scheme="mesh">Macrolides/pharmacology</classCode>
<classCode scheme="mesh">RNA, Small Interfering/metabolism</classCode>
<classCode scheme="mesh">RNA, Small Interfering/pharmacology</classCode>
<classCode scheme="mesh">Viral Envelope Proteins/metabolism*</classCode>
<classCode scheme="mesh">Clathrin/metabolism*</classCode>
<classCode scheme="mesh">Dopamine Antagonists/pharmacology</classCode>
<classCode scheme="mesh">Endocytosis*/drug effects</classCode>
<classCode scheme="mesh">Endosomes/metabolism*</classCode>
<classCode scheme="mesh">Endosomes/virology</classCode>
<classCode scheme="mesh">Enzyme Inhibitors/pharmacology</classCode>
<classCode scheme="mesh">Gene Expression Regulation, Viral/drug effects</classCode>
<classCode scheme="mesh">Hepacivirus/metabolism*</classCode>
<classCode scheme="halDomain" n="sdv.mp.vir">Life Sciences [q-bio]/Microbiology and Parasitology/Virology</classCode>
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<abstract xml:lang="en"> <p>Due to difficulties in cell culture propagation, the mechanisms of hepatitis C virus (HCV) entry are poorly understood. Here, postbinding cellular mechanisms of HCV entry were studied using both retroviral particles pseudotyped with HCV envelope glycoproteins (HCVpp) and the HCV clone JFH-1 propagated in cell culture (HCVcc). HCVpp entry was measured by quantitative real-time PCR after 3 h of contact with target cells, and HCVcc infection was quantified by immunoblot analysis and immunofluorescence detection of HCV proteins expressed in infected cells. The functional role of clathrin-mediated endocytosis in HCV entry was assessed by small interfering RNA-mediated clathrin heavy chain depletion and with chlorpromazine, an inhibitor of clathrin-coated pit formation at the plasma membrane. In both conditions, HCVpp entry and HCVcc infection were inhibited. HCVcc infection was also inhibited by pretreating target cells with bafilomycin A1 or chloroquine, two drugs known to interfere with endosome acidification. These data indicate that HCV enters target cells by clathrin-mediated endocytosis, followed by a fusion step from within an acidic endosomal compartment.</p>
</abstract>
<particDesc> <org type="consortium">We thank Laetitia Corset and Anne Goffard for help with real-time PCR. We are grateful to J. F. Delagneau, A. Patel, and J. McKeating for providing us with antibodies, D. Lavillette and F.-L. Cosset for plasmids, and L. Roux and F. Lafont for the purified stock of SeV. Some data were generated with the help of the Imaging Core Facility of the Calmette campus.</org>
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