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Binding of Lassa virus perturbs extracellular matrix-induced signal transduction via dystroglycan

Jillian M Rojek1, Marie-Laurence Moraz, Christelle Pythoud

  • 1Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.

Cellular Microbiology
|March 13, 2012
PubMed

Insights

Lassa virus (LASV) binds to dystroglycan (DG), forming an inactive signaling complex. This binding perturbs alpha6beta1 integrin signaling, impacting cell-matrix interactions crucial for LASV infection.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Lassa virus (LASV) causes severe hemorrhagic fever with high mortality.
  • Dystroglycan (DG) serves as the cellular receptor for LASV.
  • DG interacts with β1 integrins, regulating cell-matrix interactions.

Purpose of the Study:

  • To investigate if LASV binding to DG triggers signal transduction pathways.
  • To understand how LASV binding to DG affects cellular signaling.
  • To elucidate the role of DG-integrin crosstalk in LASV infection.

Main Methods:

  • Investigated LASV engagement with DG and subsequent protein recruitment.
  • Analyzed MEK/ERK pathway activation upon LASV-DG interaction.
  • Studied the impact of LASV binding on α6β1 integrin signaling.

Main Results:

  • LASV binding to DG recruited Grb2 and MEK1, forming an inactive signaling complex.
  • LASV binding did not activate the MEK/ERK pathway through DG.
  • LASV binding significantly affected MEK/ERK pathway activation via α6β1 integrins.

Conclusions:

  • LASV binding to DG initiates an inactive signaling complex.
  • LASV perturbs α6β1 integrin signaling through its interaction with DG.
  • This virus-induced signaling crosstalk is critical for LASV pathogenesis.

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