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Characterization of the interaction of lassa fever virus with its cellular receptor alpha-dystroglycan

Academic Article
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Overview

authors

  • Kunz, S.
  • Rojek, J. M.
  • Perez, M.
  • Spiropoulou, C. F.
  • Oldstone, Michael

publication date

  • May 2005

journal

  • Journal of Virology  Journal

abstract

  • The cellular receptor for the Old World arenaviruses Lassa fever virus (LFV) and lymphocytic choriomeningitis virus (LCMV) has recently been identified as alpha-dystroglycan (alpha-DG), a cell surface receptor that provides a molecular link between the extracellular matrix and the actin-based cytoskeleton. In the present study, we show that LFV binds to alpha-DG with high affinity in the low-nanomolar range. Recombinant vesicular stomatitis virus pseudotyped with LFV glycoprotein (GP) adopted the receptor binding characteristics of LFV and depended on alpha-DG for infection of cells. Mapping of the binding site of LFV on alpha-DG revealed that LFV binding required the same domains of alpha-DG that are involved in the binding of LCMV. Further, LFV was found to efficiently compete with laminin alpha1 and alpha2 chains for alpha-DG binding. Together with our previous studies on receptor binding of the prototypic immunosuppressive LCMV isolate LCMV clone 13, these findings indicate a high degree of conservation in the receptor binding characteristics between the highly human-pathogenic LFV and murine-immunosuppressive LCMV isolates.

subject areas

  • Binding Sites
  • Dystroglycans
  • HeLa Cells
  • Humans
  • Lassa Fever
  • Lassa virus
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Virus
  • Virus Replication
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Identity

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.79.10.5979-5987.2005

PubMed ID

  • 15857984
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Additional Document Info

start page

  • 5979

end page

  • 5987

volume

  • 79

issue

  • 10

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