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Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan

Marie-Laurence Moraz1, Christelle Pythoud, Rolf Turk

  • 1Institute of Microbiology, Lausanne University Hospital and University of Lausanne, Lausanne, Switzerland.

Cellular Microbiology
|January 3, 2013
PubMed

Insights

Lassa virus uses dystroglycan (DG) to enter cells. Virus binding triggers DG tyrosine phosphorylation, which disrupts utrophin binding, aiding viral entry.

Area of Science:

  • Virology
  • Cell Biology
  • Biochemistry

Background:

  • Dystroglycan (DG) is an extracellular matrix receptor.
  • DG links the extracellular matrix to the actin cytoskeleton via utrophin/dystrophin.
  • Lassa virus (LASV) uses DG as its cellular receptor.

Purpose of the Study:

  • Investigate post-translational modifications of DG during LASV cell entry.
  • Determine the role of tyrosine kinases in LASV-DG interactions.

Main Methods:

  • Utilized the tyrosine kinase inhibitor genistein.
  • Examined virus-receptor binding and particle internalization.
  • Analyzed DG tyrosine phosphorylation upon LASV glycoprotein (GP) engagement.
  • Assessed utrophin dissociation from DG.

Main Results:

  • Tyrosine kinases are essential for LASV particle internalization, not initial binding.
  • LASV GP binding to DG induces tyrosine phosphorylation of DG's cytoplasmic domain.
  • LASV GP binding causes utrophin dissociation from DG.
  • Genistein treatment impacts virus-induced utrophin dissociation, implicating tyrosine phosphorylation.

Conclusions:

  • LASV entry involves tyrosine phosphorylation of dystroglycan.
  • This phosphorylation event is critical for disrupting the DG-utrophin interaction.
  • Targeting these modifications could offer strategies against Lassa virus.

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