PubMed:22156524 JSONTXT

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":126,"end":138},"obj":"gene:1605"},{"id":"T1","span":{"begin":191,"end":202},"obj":"disease:C0023092"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Identification of cell surface molecules involved in dystroglycan-independent Lassa virus cell entry.\nAlthough 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."}

{"project":"Allie","denotations":[{"id":"SS1_22156524_2_0","span":{"begin":377,"end":455},"obj":"expanded"},{"id":"SS2_22156524_2_0","span":{"begin":457,"end":464},"obj":"abbr"}],"relations":[{"id":"AE1_22156524_2_0","pred":"abbreviatedTo","subj":"SS1_22156524_2_0","obj":"SS2_22156524_2_0"}],"text":"Identification of cell surface molecules involved in dystroglycan-independent Lassa virus cell entry.\nAlthough 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."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":197,"end":202},"obj":"HP_0001945"}],"text":"Identification of cell surface molecules involved in dystroglycan-independent Lassa virus cell entry.\nAlthough 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."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"22156524-1#24#36#gene1605","span":{"begin":126,"end":138},"obj":"gene1605"},{"id":"22156524-1#89#100#diseaseC0023092","span":{"begin":191,"end":202},"obj":"diseaseC0023092"}],"relations":[{"id":"24#36#gene160589#100#diseaseC0023092","pred":"associated_with","subj":"22156524-1#24#36#gene1605","obj":"22156524-1#89#100#diseaseC0023092"}],"text":"Identification of cell surface molecules involved in dystroglycan-independent Lassa virus cell entry.\nAlthough 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."}