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Hepatitis C virus interacts with human platelet glycoprotein VI
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Zeitschriftentitel: | Journal of General Virology |
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Personen und Körperschaften: | , , , |
In: | Journal of General Virology, 87, 2006, 8, S. 2243-2251 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Microbiology Society
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Schlagwörter: |
author_facet |
Zahn, Astrid Jennings, Nicola Ouwehand, Willem H. Allain, Jean-Pierre Zahn, Astrid Jennings, Nicola Ouwehand, Willem H. Allain, Jean-Pierre |
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author |
Zahn, Astrid Jennings, Nicola Ouwehand, Willem H. Allain, Jean-Pierre |
spellingShingle |
Zahn, Astrid Jennings, Nicola Ouwehand, Willem H. Allain, Jean-Pierre Journal of General Virology Hepatitis C virus interacts with human platelet glycoprotein VI Virology |
author_sort |
zahn, astrid |
spelling |
Zahn, Astrid Jennings, Nicola Ouwehand, Willem H. Allain, Jean-Pierre 0022-1317 1465-2099 Microbiology Society Virology http://dx.doi.org/10.1099/vir.0.81826-0 <jats:p> <jats:italic>Hepatitis C virus</jats:italic> (HCV) interacts with human platelets <jats:italic>in vivo</jats:italic> as a potential transport of infectious virions to the target liver. The binding of native viral particles with the platelet membrane glycoprotein VI (GPVI) was analysed. A consistent interaction between HCV from plasma or after purification by two different methods and the recombinant extracellular immunoglobulin (Ig)-like domains of human GPVI (hD1D2) was observed with two independent experimental approaches: pull-down and ELISA assays. Between 2 and 7 % of HCV particles were specifically bound to hD1D2. The binding was inhibited by an anti-hD1D2 in a dose-dependent manner. Human D1D2 interaction with HCV was significantly higher than the murine D1D2, supporting the specificity of the interaction and to the single human domains (D1 and D2), suggesting that both Ig-like domains of the molecule are required for efficient binding. GPVI may be a platelet surface ligand for HCV playing a role in viral transport and persistence.</jats:p> Hepatitis C virus interacts with human platelet glycoprotein VI Journal of General Virology |
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10.1099/vir.0.81826-0 |
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Microbiology Society, 2006 |
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Microbiology Society, 2006 |
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0022-1317 1465-2099 |
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0022-1317 1465-2099 |
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Microbiology Society |
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Journal of General Virology |
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title |
Hepatitis C virus interacts with human platelet glycoprotein VI |
title_unstemmed |
Hepatitis C virus interacts with human platelet glycoprotein VI |
title_full |
Hepatitis C virus interacts with human platelet glycoprotein VI |
title_fullStr |
Hepatitis C virus interacts with human platelet glycoprotein VI |
title_full_unstemmed |
Hepatitis C virus interacts with human platelet glycoprotein VI |
title_short |
Hepatitis C virus interacts with human platelet glycoprotein VI |
title_sort |
hepatitis c virus interacts with human platelet glycoprotein vi |
topic |
Virology |
url |
http://dx.doi.org/10.1099/vir.0.81826-0 |
publishDate |
2006 |
physical |
2243-2251 |
description |
<jats:p>
<jats:italic>Hepatitis C virus</jats:italic> (HCV) interacts with human platelets <jats:italic>in vivo</jats:italic> as a potential transport of infectious virions to the target liver. The binding of native viral particles with the platelet membrane glycoprotein VI (GPVI) was analysed. A consistent interaction between HCV from plasma or after purification by two different methods and the recombinant extracellular immunoglobulin (Ig)-like domains of human GPVI (hD1D2) was observed with two independent experimental approaches: pull-down and ELISA assays. Between 2 and 7 % of HCV particles were specifically bound to hD1D2. The binding was inhibited by an anti-hD1D2 in a dose-dependent manner. Human D1D2 interaction with HCV was significantly higher than the murine D1D2, supporting the specificity of the interaction and to the single human domains (D1 and D2), suggesting that both Ig-like domains of the molecule are required for efficient binding. GPVI may be a platelet surface ligand for HCV playing a role in viral transport and persistence.</jats:p> |
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author | Zahn, Astrid, Jennings, Nicola, Ouwehand, Willem H., Allain, Jean-Pierre |
author_facet | Zahn, Astrid, Jennings, Nicola, Ouwehand, Willem H., Allain, Jean-Pierre, Zahn, Astrid, Jennings, Nicola, Ouwehand, Willem H., Allain, Jean-Pierre |
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container_title | Journal of General Virology |
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description | <jats:p> <jats:italic>Hepatitis C virus</jats:italic> (HCV) interacts with human platelets <jats:italic>in vivo</jats:italic> as a potential transport of infectious virions to the target liver. The binding of native viral particles with the platelet membrane glycoprotein VI (GPVI) was analysed. A consistent interaction between HCV from plasma or after purification by two different methods and the recombinant extracellular immunoglobulin (Ig)-like domains of human GPVI (hD1D2) was observed with two independent experimental approaches: pull-down and ELISA assays. Between 2 and 7 % of HCV particles were specifically bound to hD1D2. The binding was inhibited by an anti-hD1D2 in a dose-dependent manner. Human D1D2 interaction with HCV was significantly higher than the murine D1D2, supporting the specificity of the interaction and to the single human domains (D1 and D2), suggesting that both Ig-like domains of the molecule are required for efficient binding. GPVI may be a platelet surface ligand for HCV playing a role in viral transport and persistence.</jats:p> |
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spelling | Zahn, Astrid Jennings, Nicola Ouwehand, Willem H. Allain, Jean-Pierre 0022-1317 1465-2099 Microbiology Society Virology http://dx.doi.org/10.1099/vir.0.81826-0 <jats:p> <jats:italic>Hepatitis C virus</jats:italic> (HCV) interacts with human platelets <jats:italic>in vivo</jats:italic> as a potential transport of infectious virions to the target liver. The binding of native viral particles with the platelet membrane glycoprotein VI (GPVI) was analysed. A consistent interaction between HCV from plasma or after purification by two different methods and the recombinant extracellular immunoglobulin (Ig)-like domains of human GPVI (hD1D2) was observed with two independent experimental approaches: pull-down and ELISA assays. Between 2 and 7 % of HCV particles were specifically bound to hD1D2. The binding was inhibited by an anti-hD1D2 in a dose-dependent manner. Human D1D2 interaction with HCV was significantly higher than the murine D1D2, supporting the specificity of the interaction and to the single human domains (D1 and D2), suggesting that both Ig-like domains of the molecule are required for efficient binding. GPVI may be a platelet surface ligand for HCV playing a role in viral transport and persistence.</jats:p> Hepatitis C virus interacts with human platelet glycoprotein VI Journal of General Virology |
spellingShingle | Zahn, Astrid, Jennings, Nicola, Ouwehand, Willem H., Allain, Jean-Pierre, Journal of General Virology, Hepatitis C virus interacts with human platelet glycoprotein VI, Virology |
title | Hepatitis C virus interacts with human platelet glycoprotein VI |
title_full | Hepatitis C virus interacts with human platelet glycoprotein VI |
title_fullStr | Hepatitis C virus interacts with human platelet glycoprotein VI |
title_full_unstemmed | Hepatitis C virus interacts with human platelet glycoprotein VI |
title_short | Hepatitis C virus interacts with human platelet glycoprotein VI |
title_sort | hepatitis c virus interacts with human platelet glycoprotein vi |
title_unstemmed | Hepatitis C virus interacts with human platelet glycoprotein VI |
topic | Virology |
url | http://dx.doi.org/10.1099/vir.0.81826-0 |