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

Virology. 2003 Nov 25;316(2):213-20. doi: 10.1016/j.virol.2003.07.002.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cricetinae
  • Cytoskeletal Proteins / physiology*
  • Dystroglycans
  • Lymphocytic Choriomeningitis / etiology*
  • Membrane Glycoproteins / physiology*
  • Receptors, Virus / physiology*


  • Cytoskeletal Proteins
  • Membrane Glycoproteins
  • Receptors, Virus
  • Dystroglycans