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Alpha-dystroglycan can mediate arenavirus infection in the absence of beta-dystroglycan

Academic Article
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Overview

authors

  • Kunz, S.
  • Campbell, K. P.
  • Oldstone, Michael

publication date

  • November 2003

journal

  • Virology  Journal

abstract

  • Dystroglycan (DG) is a highly versatile cell surface molecule that provides a molecular link between the extracellular matrix (ECM) and the actin-based cytoskeleton. Encoded by a single gene, DG is posttranslationally processed to form alpha-DG, a peripheral protein identified as the cellular receptor for lymphocytic choriomeningitis virus (LCMV) and Lassa fever virus (LFV), and the membrane-spanning subunit beta-DG. The link of beta-DG to the actin-based cytoskeleton and its association with the cellular signal transduction network suggest that it may function as an essential cofactor for the activity of alpha-DG as a virus receptor. To address this issue, we constructed a deletion mutant lacking the cytoplasmic domain of beta-DG and a C-terminal fusion between alpha-DG and the transmembrane domain of PDGF receptor. Both mutants were functional as virus receptors, indicating that beta-DG does not act as a cofactor with alpha-DG for arenavirus binding and entry. These observations are in agreement with the fact that LCMV infection is independent from the structural integrity of the actin-based cytoskeleton and suggest that alpha-DG functions primarily in the attachment of arenaviruses to the cell surface.

subject areas

  • Animals
  • Cricetinae
  • Cytoskeletal Proteins
  • Dystroglycans
  • Lymphocytic Choriomeningitis
  • Membrane Glycoproteins
  • Receptors, Virus
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Research

keywords

  • dystroglycan
  • lymphocytic choriomeningitis virus
  • receptor
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Identity

International Standard Serial Number (ISSN)

  • 0042-6822

Digital Object Identifier (DOI)

  • 10.1016/s0042-6822(03)00592-0

PubMed ID

  • 14644604
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Additional Document Info

start page

  • 213

end page

  • 220

volume

  • 316

issue

  • 2

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