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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-49280

Wohlschlager, T; Butschi, A; Zurfluh, K; Vonesch, S C; Auf dem Keller, U; Gehrig, P; Bleuler-Martinez, S; Hengartner, M O; Aebi, M; Künzler, M (2011). Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity. Journal of Biological Chemistry, 286(35):30337-30343.

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Abstract

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 Galα1,3Gal/GalNAc-specific lectin from the fairy ring mushroom that consists of an N-terminal ricin B-type lectin domain and a C-terminal dimerization domain. The latter domain shows structural similarity to catalytically active proteins, suggesting that, in addition to its carbohydrate-binding activity, MOA has an enzymatic function. Here, we demonstrate toxicity of MOA toward the model nematode Caenorhabditis elegans. This toxicity depends on binding of MOA to glycosphingolipids of the worm via its lectin domain. We show further that MOA has cysteine protease activity and demonstrate a critical role of this catalytic function in MOA-mediated nematotoxicity. The proteolytic activity of MOA was dependent on high Ca(2+) concentrations and favored by slightly alkaline pH, suggesting that these conditions trigger activation of the toxin at the target location. Our results suggest that MOA is a fungal toxin with intriguing similarities to bacterial binary toxins and has a protective function against fungivorous soil nematodes.

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Functional Genomics Center Zurich
07 Faculty of Science > Institute of Molecular Life Sciences
DDC:570 Life sciences; biology
610 Medicine & health
Language:English
Date:8 July 2011
Deposited On:06 Sep 2011 13:19
Last Modified:15 Jun 2014 07:32
Publisher:American Society for Biochemistry and Molecular Biology
ISSN:0021-9258
Publisher DOI:10.1074/jbc.M111.258202
PubMed ID:21757752
Citations:Web of Science®. Times Cited: 6
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Scopus®. Citation Count: 6

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