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Posttranslational modification of alpha-dystroglycan, the cellular receptor for arenaviruses, by the glycosyltransferase large is critical for virus binding

Academic Article
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Overview

authors

  • Kunz, S.
  • Rojek, J. M.
  • Kanagawa, M.
  • Spiroroulou, C. F.
  • Barresi, R.
  • Campbell, K. P.
  • Oldstone, Michael

publication date

  • November 2005

journal

  • Journal of Virology  Journal

abstract

  • The receptor for lymphocytic choriomeningitis virus (LCMV), the human pathogenic Lassa fever virus (LFV), and clade C New World arenaviruses is alpha-dystroglycan (alpha-DG), a cell surface receptor for proteins of the extracellular matrix (ECM). Specific posttranslational modification of alpha-DG by the glycosyltransferase LARGE is critical for its function as an ECM receptor. In the present study, we show that LARGE-dependent modification is also crucial for alpha-DG's function as a cellular receptor for arenaviruses. Virus binding involves the mucin-type domain of alpha-DG and depends on modification by LARGE. A crucial role of the LARGE-dependent glycosylation of alpha-DG for virus binding is found for several isolates of LCMV, LFV, and the arenaviruses Mobala and Oliveros. Since the posttranslational modification by LARGE is crucial for alpha-DG recognition by both arenaviruses and the host-derived ligand laminin, it also influences competition between virus and laminin for alpha-DG. Hence, LARGE-dependent glycosylation of alpha-DG has important implications for the virus-host cell interaction and the pathogenesis of LFV in humans.

subject areas

  • Animals
  • Arenaviridae
  • Base Sequence
  • Crosses, Genetic
  • DNA Primers
  • DNA-Directed RNA Polymerases
  • Dystroglycans
  • Female
  • Kinetics
  • Male
  • Mice
  • Mice, Inbred C57BL
  • N-Acetylglucosaminyltransferases
  • Protein Processing, Post-Translational
  • Viral Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.79.22.14282-14296.2005

PubMed ID

  • 16254363
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Additional Document Info

start page

  • 14282

end page

  • 14296

volume

  • 79

issue

  • 22

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