Identification of cell surface molecules involved in dystroglycan-independent Lassa virus cell entry.

Article Details

Citation

Shimojima M, Stroher U, Ebihara H, Feldmann H, Kawaoka Y

Identification of cell surface molecules involved in dystroglycan-independent Lassa virus cell entry.

J Virol. 2012 Feb;86(4):2067-78. doi: 10.1128/JVI.06451-11. Epub 2011 Dec 7.

PubMed ID
22156524 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Tyrosine-protein kinase receptor TYRO3Q06418Details
Tyrosine-protein kinase receptor UFOP30530Details