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Updated: Mar 30, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
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.
Background:
Fruiting body lectins have been proposed to act as effector proteins in the defense of fungi against parasites and predators. The Marasmius oreades agglutinin (MOA) is a lectin from the fairy ring mushroom with specificity for Galα1-3Gal containing carbohydrates. This lectin is composed of an N-terminal carbohydrate-binding domain and a C-terminal dimerization domain. The dimerization domain of MOA shows in addition calcium-dependent cysteine protease activity, similar to the calpain family.
Methods:
Cell detachment assay, cell viability assay, immunofluorescence, live cell imaging and Western blot using MDCKII cell line.
Results:
In this study, we demonstrate in MDCKII cells that after internalization, MOA protease activity induces profound physiological cellular responses, like cytoskeleton rearrangement, cell detachment and cell death. These changes are preceded by a decrease in FAK phosphorylation and an internalization and degradation of β1-integrin, consistent with a disruption of integrin-dependent cell adhesion signaling. Once internalized, MOA accumulates in late endosomal compartments.
Conclusion:
Our results suggest a possible toxic mechanism of MOA, which consists of disturbing the cell adhesion and the cell viability.
General Significance:
After being ingested by a predator, MOA might exert a protective role by diminishing host cell integrity.
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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