author_facet Shimojima, Masayuki
Ströher, Ute
Ebihara, Hideki
Feldmann, Heinz
Kawaoka, Yoshihiro
Shimojima, Masayuki
Ströher, Ute
Ebihara, Hideki
Feldmann, Heinz
Kawaoka, Yoshihiro
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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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
container_issue 4
container_start_page 2067
container_title Journal of Virology
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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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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