The Fungal Chimerolectin MOA Inhibits Protein and DNA Synthesis in NIH/3T3 Cells and May Induce BAX-Mediated Apoptosis
Cordara et al., Biochemical and Biophysical Research Communications (2014) - PMID: 24747075
Product(s) used in this publication: Peptide Microarray Assay Services
The Marasmius oreades mushroom agglutinin (MOA) is a blood group B-specific lectin carrying an active proteolytic domain. Its enzymatic activity has recently been shown to be critical for toxicity of MOA toward the fungivorous soil nematode Caenorhabditis elegans. Here we present evidence that MOA also induces cytotoxicity in a cellular model system (murine NIH/3T3 cells), by inhibiting protein synthesis, and that cytotoxicity correlates, at least in part, with proteolytic activity. A peptide-array screen identified the apoptosis mediator BAX as a potential proteolytic substrate and further suggests a variety of bacterial and fungal peptides as potential substrates. These findings are in line with the suggestion that MOA and related proteases may play a role for host defense.
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Cystein protease; Cytotoxicity; Fungal chimerolectin; Hydrolytic enzyme; NIH/3T3 cells