2012
DOI: 10.1371/journal.ppat.1002706
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Plasticity of the β-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence System

Abstract: Discrimination between self and non-self is a prerequisite for any defence mechanism; in innate defence, this discrimination is often mediated by lectins recognizing non-self carbohydrate structures and so relies on an arsenal of host lectins with different specificities towards target organism carbohydrate structures. Recently, cytoplasmic lectins isolated from fungal fruiting bodies have been shown to play a role in the defence of multicellular fungi against predators and parasites. Here, we present a novel … Show more

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Cited by 75 publications
(131 citation statements)
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“…In addition to these canonical sites, the β-trefoil fold can also harbor noncanonical carbohydrate-binding sites (Schubert et al 2012) and, as in case of protease inhibitors, binding sites for proteases (Žurga et al 2015) (see below). The best characterized representatives of this family of mushroom lectins are Rhizoctonia solani agglutinin (RSA) and Sclerotinia sclerotiorum agglutinin (SSA) of the plant pathogens R. solani (basidiomycete) (Hamshou et al 2013) and S. sclerotiorum (ascomycete) (Sulzenbacher et al 2010), as well as CNL, CCL2, MpL, and BEL β-trefoil of the homobasidio(agarico)mycetes Clitocybe nebularis (Pohleven et al 2009;Pohleven et al 2012), C. cinerea (Schubert et al 2012), Macrolepiota procera (Žurga et al 2014), and Boletus edulis (Bovi et al 2013) (Table 1). These proteins show high sequence variability, as they share only 7 to 16 % sequence identity (25 to 35 % similarity), the exception being CNL, MpL, and RSA that are 23 to 26 % identical (30 to 40 % similar).…”
Section: β-Trefoil-type Lectinsmentioning
confidence: 99%
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“…In addition to these canonical sites, the β-trefoil fold can also harbor noncanonical carbohydrate-binding sites (Schubert et al 2012) and, as in case of protease inhibitors, binding sites for proteases (Žurga et al 2015) (see below). The best characterized representatives of this family of mushroom lectins are Rhizoctonia solani agglutinin (RSA) and Sclerotinia sclerotiorum agglutinin (SSA) of the plant pathogens R. solani (basidiomycete) (Hamshou et al 2013) and S. sclerotiorum (ascomycete) (Sulzenbacher et al 2010), as well as CNL, CCL2, MpL, and BEL β-trefoil of the homobasidio(agarico)mycetes Clitocybe nebularis (Pohleven et al 2009;Pohleven et al 2012), C. cinerea (Schubert et al 2012), Macrolepiota procera (Žurga et al 2014), and Boletus edulis (Bovi et al 2013) (Table 1). These proteins show high sequence variability, as they share only 7 to 16 % sequence identity (25 to 35 % similarity), the exception being CNL, MpL, and RSA that are 23 to 26 % identical (30 to 40 % similar).…”
Section: β-Trefoil-type Lectinsmentioning
confidence: 99%
“…Based on the accumulation of protein during sclerotium formation and its depletion during mycelium germination, a storage function for RSA in R. solani has been proposed. CCL2 and its paralog CCL1 exhibit a pronounced fruiting body-specific expression with almost no expression in the vegetative mycelium of C. cinerea (Plaza et al 2014;Schubert et al 2012).…”
Section: β-Trefoil-type Lectinsmentioning
confidence: 99%
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