Uptake of Marasmius oreades agglutinin disrupts integrin-dependent cell adhesion

Samuel Juillot1, Catherine Cott2, Josef Madl2

  • 1Faculty of Biology, Albert-Ludwigs-University Freiburg, Schänzlestraße 1, D-79104 Freiburg, Germany; Spemann Graduate School of Biology and Medicine (SGBM), Albert-Ludwigs-University Freiburg, D-79104 Freiburg, Germany; BIOSS-Centre for Biological Signalling Studies, Albert-Ludwigs-University Freiburg, Schänzlestraße 18, D-79104 Freiburg, Germany.

Abstract

Insights

The Marasmius oreades agglutinin (MOA) lectin disrupts cell adhesion and viability by degrading beta1-integrin. This fungal protein may protect against predators by compromising host cell integrity.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Mycology

Background:

  • Fruiting body lectins, like Marasmius oreades agglutinin (MOA), are implicated in fungal defense mechanisms.
  • MOA is a lectin specific for Galα1-3Gal carbohydrates, featuring a carbohydrate-binding domain and a calcium-dependent cysteine protease domain.

Purpose of the Study:

  • To investigate the cellular effects and toxic mechanisms of the Marasmius oreades agglutinin (MOA) lectin in mammalian cells.
  • To elucidate the role of MOA's protease activity in cellular responses.

Main Methods:

  • Utilized Madin-Darby Canine Kidney II (MDCKII) cell line for experiments.
  • Employed cell detachment assays, cell viability assays, immunofluorescence, live cell imaging, and Western blotting.

Main Results:

  • Internalized MOA protease activity triggers cytoskeleton rearrangement, cell detachment, and cell death in MDCKII cells.
  • MOA disrupts integrin-dependent cell adhesion signaling, evidenced by decreased FAK phosphorylation and beta1-integrin internalization/degradation.
  • Internalized MOA localizes to late endosomal compartments within the cell.

Conclusions:

  • MOA exhibits a toxic mechanism by interfering with cell adhesion and viability.
  • MOA may provide a protective role for fungi by compromising host cell integrity upon ingestion by predators.

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