Insecticidal properties of Sclerotinia sclerotiorum agglutinin and its interaction with insect tissues and cells

Hamshou, Mohamad; Smagghe, Guy; Shahidi-Noghabi, Shahnaz; Geyter, Ellen De; Lannoo, Nausicaä; Damme, Els J.M. Van

doi:10.1016/j.ibmb.2010.08.008

Cited by 47 publications

(51 citation statements)

References 56 publications

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“…SSA is highly toxic toward the pea aphid Acyrthosiphon pisum. It binds to the insect midgut cells and, like RSA, is not internalized but causes death of midgut epithelial cells probably via a signal transduction pathway triggered by a glycoreceptor (Hamshou et al 2010a). In contrast, CCL2 is not toxic for insects but exhibits strong toxicity toward C. elegans.…”

Section: β-Trefoil-type Lectinsmentioning

confidence: 99%

“…Furthermore, the effect of different fungal lectins against the important sap sucking crop pests, using pea aphid A. pisum as a model organism, has been analyzed. The β-trefoil lectin SSA exhibited strong toxicity in feeding assays (Hamshou et al 2010a). Actinoporin-type lectin XCL also exhibited toxicity against aphids including A. pisum and green peach aphid (M. persicae) (Jaber et al 2007;Jaber et al 2006;Trigueros et al 2003).…”

Section: Potential Applicationsmentioning

confidence: 99%

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Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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Fruiting bodies or sporocarps of dikaryotic (ascomycetous and basidiomycetous) fungi, commonly referred to as mushrooms, are often rich in entomotoxic and nematotoxic proteins that include lectins and protease inhibitors. These protein toxins are thought to act as effectors of an innate defense system of mushrooms against animal predators including fungivorous insects and nematodes. In this review, we summarize current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin-type lectins, beta-propeller-type lectins and beta-trefoil-type chimerolectins, as well as mycospin and mycocypin families of protease inhibitors. We also present an overview of the phylogenetic distribution of these proteins among a selection of fungal genomes and draw some conclusions about their evolution and physiological function. Finally, we present an outlook for future research directions in this field and their potential applications in medicine and crop protection.

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Section: β-Trefoil-type Lectinsmentioning

confidence: 99%

Section: Potential Applicationsmentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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“…A recent study that investigated the mechanism of action of lectins at the cellular level was able to demonstrate that binding of lectins (ribosome-inactivating proteins or legume lectin) to the midgut epithelium appeared to induce severe anatomical abnormalities with pathological consequences, such as apoptosis of epithelial cells, which may explain their cytotoxicity (Hamshou et al 2010;Shahidi-Noghabi et al 2010a;Sprawka et al 2013). Apoptosis is a physiological mechanism that is required to maintain cell numbers and remove unnecessary cells.…”

Section: Introductionmentioning

confidence: 99%

Apoptosis induction by concanavalin A in gut cells of grain aphid

Sprawka

Goławska

Parzych

et al. 2015

Arthropod-Plant Interactions

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In this study, the toxicity and mechanism of action of concanavalin A (ConA) in the grain aphid (Sitobion avenae) were studied. Feeding assays with S. avenae on an artificial diet containing different concentrations of ConA demonstrated an inhibitory effect on fecundity as well as high mortality caused by this lectin. ConA also increased the pre-reproductive period and the development time and reduced the intrinsic rate of natural increase. Moreover, an extract of the gut of treated S. avenae demonstrated an increase in caspase-3 activity together with DNA fragmentation, suggesting that ConA can induce the apoptotic pathway. These results suggest that ConA may be detrimental in insect gut tissues and the interaction of ConA with epithelial cells may be responsible for the observed insecticidal effects.

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“…The exclusive and abundant expression of these lectins in fruiting bodies or sclerotia of the host fungus may result in special protection of these reproductive organs. It is proposed that predators such as fungivorous nematodes ingest the cytoplasmic lectin when feeding on the content of the fungal cell and that binding of the lectin to specific glycans in the intestine of the worm induces toxicity by an unknown mechanism (2)(3)(4)(5).…”

mentioning

confidence: 99%

Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity

Wohlschlager¹,

Butschi

Zurfluh³

et al. 2011

Journal of Biological Chemistry

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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 Gal␣1,3Gal/ 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.

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Insecticidal properties of Sclerotinia sclerotiorum agglutinin and its interaction with insect tissues and cells

Cited by 47 publications

References 56 publications

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Apoptosis induction by concanavalin A in gut cells of grain aphid

Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity

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