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Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry
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Zeitschriftentitel: | Journal of Virology |
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Personen und Körperschaften: | , , , , |
In: | Journal of Virology, 86, 2012, 4, S. 2067-2078 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
American Society for Microbiology
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Schlagwörter: |
author_facet |
Shimojima, Masayuki Ströher, Ute Ebihara, Hideki Feldmann, Heinz Kawaoka, Yoshihiro Shimojima, Masayuki Ströher, Ute Ebihara, Hideki Feldmann, Heinz Kawaoka, Yoshihiro |
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author |
Shimojima, Masayuki Ströher, Ute Ebihara, Hideki Feldmann, Heinz Kawaoka, Yoshihiro |
spellingShingle |
Shimojima, Masayuki Ströher, Ute Ebihara, Hideki Feldmann, Heinz Kawaoka, Yoshihiro Journal of Virology Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry Virology Insect Science Immunology Microbiology |
author_sort |
shimojima, masayuki |
spelling |
Shimojima, Masayuki Ströher, Ute Ebihara, Hideki Feldmann, Heinz Kawaoka, Yoshihiro 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.06451-11 <jats:title>ABSTRACT</jats:title> <jats:p>Although O-mannosylated dystroglycan is a receptor for Lassa virus, a causative agent of Lassa fever, recent findings suggest the existence of an alternative receptor(s). Here we identified four molecules as receptors for Lassa virus: Axl and Tyro3, from the TAM family, and dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) and liver and lymph node sinusoidal endothelial calcium-dependent lectin (LSECtin), from the C-type lectin family. These molecules enhanced the binding of Lassa virus to cells and mediated infection independently of dystroglycan. Axl- or Tyro3-mediated infection required intracellular signaling via the tyrosine kinase activity of Axl or Tyro3, whereas DC-SIGN- or LSECtin-mediated infection and binding were dependent on a specific carbohydrate and on ions. The identification of these four molecules as Lassa virus receptors advances our understanding of Lassa virus cell entry.</jats:p> Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry Journal of Virology |
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10.1128/jvi.06451-11 |
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American Society for Microbiology, 2012 |
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American Society for Microbiology, 2012 |
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2012 |
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American Society for Microbiology |
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Journal of Virology |
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title |
Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_unstemmed |
Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_full |
Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_fullStr |
Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_full_unstemmed |
Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_short |
Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_sort |
identification of cell surface molecules involved in dystroglycan-independent lassa virus cell entry |
topic |
Virology Insect Science Immunology Microbiology |
url |
http://dx.doi.org/10.1128/jvi.06451-11 |
publishDate |
2012 |
physical |
2067-2078 |
description |
<jats:title>ABSTRACT</jats:title>
<jats:p>Although O-mannosylated dystroglycan is a receptor for Lassa virus, a causative agent of Lassa fever, recent findings suggest the existence of an alternative receptor(s). Here we identified four molecules as receptors for Lassa virus: Axl and Tyro3, from the TAM family, and dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) and liver and lymph node sinusoidal endothelial calcium-dependent lectin (LSECtin), from the C-type lectin family. These molecules enhanced the binding of Lassa virus to cells and mediated infection independently of dystroglycan. Axl- or Tyro3-mediated infection required intracellular signaling via the tyrosine kinase activity of Axl or Tyro3, whereas DC-SIGN- or LSECtin-mediated infection and binding were dependent on a specific carbohydrate and on ions. The identification of these four molecules as Lassa virus receptors advances our understanding of Lassa virus cell entry.</jats:p> |
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author | Shimojima, Masayuki, Ströher, Ute, Ebihara, Hideki, Feldmann, Heinz, Kawaoka, Yoshihiro |
author_facet | Shimojima, Masayuki, Ströher, Ute, Ebihara, Hideki, Feldmann, Heinz, Kawaoka, Yoshihiro, Shimojima, Masayuki, Ströher, Ute, Ebihara, Hideki, Feldmann, Heinz, Kawaoka, Yoshihiro |
author_sort | shimojima, masayuki |
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container_title | Journal of Virology |
container_volume | 86 |
description | <jats:title>ABSTRACT</jats:title> <jats:p>Although O-mannosylated dystroglycan is a receptor for Lassa virus, a causative agent of Lassa fever, recent findings suggest the existence of an alternative receptor(s). Here we identified four molecules as receptors for Lassa virus: Axl and Tyro3, from the TAM family, and dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) and liver and lymph node sinusoidal endothelial calcium-dependent lectin (LSECtin), from the C-type lectin family. These molecules enhanced the binding of Lassa virus to cells and mediated infection independently of dystroglycan. Axl- or Tyro3-mediated infection required intracellular signaling via the tyrosine kinase activity of Axl or Tyro3, whereas DC-SIGN- or LSECtin-mediated infection and binding were dependent on a specific carbohydrate and on ions. The identification of these four molecules as Lassa virus receptors advances our understanding of Lassa virus cell entry.</jats:p> |
doi_str_mv | 10.1128/jvi.06451-11 |
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spelling | Shimojima, Masayuki Ströher, Ute Ebihara, Hideki Feldmann, Heinz Kawaoka, Yoshihiro 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.06451-11 <jats:title>ABSTRACT</jats:title> <jats:p>Although O-mannosylated dystroglycan is a receptor for Lassa virus, a causative agent of Lassa fever, recent findings suggest the existence of an alternative receptor(s). Here we identified four molecules as receptors for Lassa virus: Axl and Tyro3, from the TAM family, and dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) and liver and lymph node sinusoidal endothelial calcium-dependent lectin (LSECtin), from the C-type lectin family. These molecules enhanced the binding of Lassa virus to cells and mediated infection independently of dystroglycan. Axl- or Tyro3-mediated infection required intracellular signaling via the tyrosine kinase activity of Axl or Tyro3, whereas DC-SIGN- or LSECtin-mediated infection and binding were dependent on a specific carbohydrate and on ions. The identification of these four molecules as Lassa virus receptors advances our understanding of Lassa virus cell entry.</jats:p> Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry Journal of Virology |
spellingShingle | Shimojima, Masayuki, Ströher, Ute, Ebihara, Hideki, Feldmann, Heinz, Kawaoka, Yoshihiro, Journal of Virology, Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry, Virology, Insect Science, Immunology, Microbiology |
title | Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_full | Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_fullStr | Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_full_unstemmed | Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_short | Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
title_sort | identification of cell surface molecules involved in dystroglycan-independent lassa virus cell entry |
title_unstemmed | Identification of Cell Surface Molecules Involved in Dystroglycan-Independent Lassa Virus Cell Entry |
topic | Virology, Insect Science, Immunology, Microbiology |
url | http://dx.doi.org/10.1128/jvi.06451-11 |