Correction: Plasticity of the β-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence System

Schubert, Mario; Bleuler-Martinez, Silvia; Butschi, Alex; Wälti, Marielle A.; Egloff, Pascal; Stutz, Katrin; Shi, Yan; Collot, Mayeul; Mallet, Jean-Maurice; Wilson, Iain B. H.; Hengartner, Michael O.; Aebi, Markus; Allain, FrÃ©dÃ©ric H.-T.; KÃ1⁄4nzler, Markus

doi:10.1371/annotation/ed5d46f6-3442-4a89-a505-78befd507436

Cited by 4 publications

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“…Some of these residues, e.g. Y57, W78, L87, Y92 and W94, were previously shown to be involved in binding of the trisaccharide GlcNAc(Fucα1,3)β1,4GlcNAc by the single, high-affinity binding site of CCL2 (Schubert, M., Bleuler-Martinez, S., et al 2012). The conservation of other conserved residues, e.g.…”

Section: Mutation Of a Conserved Residue Of Ccl2 (R18a) Significantly...mentioning

confidence: 99%

“…To elucidate the molecular basis behind the effect of the R18A mutation on nematotoxicity, we first verified that R18 is not involved in carbohydrate-binding. We performed an NMR titration experiment with recombinant, His-tagged protein in which we monitored binding of the previously used, synthetic ligand GlcNAc(Fucα1,3)β1,4GlcNAcβ1O(CH 2 ) 5 COOH (Schubert, M., Bleuler-Martinez, S., et al 2012) on the protein side at residue-specific precision using 2D NMR spectroscopy in combination with 15 N labeled protein (Fig. 3).…”

Section: R18a Mutation Does Not Affect Carbohydrate Bindingmentioning

confidence: 99%

“…Based on previously published NMR and size exclusion chromatography (SEC) data, it was concluded that CCL2 was monomeric (Schubert, M., Bleuler-Martinez, S., et al 2012). In contrast, six other single domain β-trefoil fungal lectins have been structurally characterized so far and been shown to form dimers such as Clitocybe nebularis lectin CNL (Pohleven, J., Renko, M., et al 2012), Boletus edulis beta-trefoil lectin BEL (Bovi, M., Cenci, L., et al 2013), Sclerotinia sclerotiorum agglutinin SSA (Sulzenbacher, G., Roig-Zamboni, V., et al 2010) and Rhizoctonia solani agglutinin RSA (Skamnaki, V.T., Peumans, W.J., et al 2013).…”

Section: X-ray Crystallography Reveals the Formation Of Ccl2 Dimersmentioning

confidence: 99%

“…Toxicity of CCL2 towards the model nematode Caenorhabditis elegans is dependent on the specific recognition of the α1,3fucosylated cores of N-glycans on the nematode intestinal epithelium but does not involve endocytosis of the lectin (Stutz, K., Kaech, A., et al 2015). The previously determined three-dimensional NMR structure of monomeric CCL2 explained how the specificity and high affinity of this protein for this unusual glycan target is achieved F o r P e e r R e v i e w (Schubert, M., Bleuler-Martinez, S., et al 2012) but gave, as a monovalent monomer, no hints at the toxicity mechanism. Here, further characterization with notably protein X-ray crystallography and NMR revealed that CCL2 forms in fact a compact dimer and, thus, is bivalent for its ligand.…”

Section: Introductionmentioning

confidence: 97%

“…An exception to these proposed mechanisms seemed to be the recently identified β-trefoil lectin CCL2 that is highly expressed in Coprinopsis cinerea fruiting bodies (Plaza, D.F., Lin, C.W., et al 2014). CCL2 has been implicated in the defense of this mushroom against invertebrate predators based on its toxicity towards nematodes and insects (Heim, C., Hertzberg, H., et al 2015, Schubert, M., Bleuler-Martinez, S., et al 2012. Toxicity of CCL2 towards the model nematode Caenorhabditis elegans is dependent on the specific recognition of the α1,3fucosylated cores of N-glycans on the nematode intestinal epithelium but does not involve endocytosis of the lectin (Stutz, K., Kaech, A., et al 2015).…”

Section: Introductionmentioning

confidence: 99%

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Dimerization of the fungal defense lectin CCL2 is essential for its toxicity against nematodes

et al. 2016

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Lectins are used as defense effector proteins against predators, parasites and pathogens by animal, plant and fungal innate defense systems. These proteins bind to specific glycoepitopes on the cell surfaces and thereby interfere with the proper cellular functions of the various antagonists. The exact cellular toxicity mechanism is in many cases unclear. Lectin CCL2 of the mushroom Coprinopsis cinerea was previously shown to be toxic for Caenorhabditis elegans and Drosophila melanogaster. This toxicity is dependent on a single, high-affinity binding site for the trisaccharide GlcNAc(Fucα1,3)β1,4GlcNAc, which is a hallmark of nematode and insect N-glycan cores. The carbohydrate-binding site is located at an unusual position on the protein surface when compared to other β-trefoil lectins. Here, we show that CCL2 forms a compact dimer in solution and in crystals. Substitution of two amino acid residues at the dimer interface, R18A and F133A, interfered with dimerization of CCL2 and reduced toxicity but left carbohydrate-binding unaffected. These results, together with the positioning of the two carbohydrate-binding sites on the surface of the protein dimer, suggest that crosslinking of N-glycoproteins on the surface of intestinal cells of invertebrates is a crucial step in the mechanism of CCL2-mediated toxicity. Comparisons of the number and positioning of carbohydrate-binding sites among different dimerizing fungal β-trefoil lectins revealed a considerable variability in the carbohydrate-binding patterns of these proteins, which are likely to correlate with their respective functions.

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Section: Mutation Of a Conserved Residue Of Ccl2 (R18a) Significantly...mentioning

confidence: 99%

Section: R18a Mutation Does Not Affect Carbohydrate Bindingmentioning

confidence: 99%

Section: X-ray Crystallography Reveals the Formation Of Ccl2 Dimersmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

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Dimerization of the fungal defense lectin CCL2 is essential for its toxicity against nematodes

et al. 2016

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Transcriptomic atlas of mushroom development highlights an independent origin of complex multicellularity

Krizsán

Almási

Merényi

et al. 2018

Preprint

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We constructed a reference atlas of mushroom formation based on developmental transcriptome data of six species and comparisons of >200 whole genomes, to elucidate the core genetic program of complex multicellularity and fruiting body development in mushroom-forming fungi (Agaricomycetes). Nearly 300 conserved gene families and >70 functional groups contained developmentally regulated genes from five to six species, covering functions related to fungal cell wall (FCW) remodeling, targeted protein degradation, signal transduction, adhesion and small secreted proteins (including effector-like orphan genes). Several of these families, including F-box proteins, protein kinases and cadherin-like proteins, showed massive expansions in Agaricomycetes, with many convergently expanded in multicellular plants and/or animals too, reflecting broad genetic convergence among independently evolved complex multicellular lineages. This study provides a novel entry point to studying mushroom development and complex multicellularity in one of the largest clades of complex eukaryotic organisms.

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Cocaprins, β-Trefoil Fold Inhibitors of Cysteine and Aspartic Proteases from Coprinopsis cinerea

Renko

Zupan

Plaza

et al. 2022

IJMS

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We introduce a new family of fungal protease inhibitors with β-trefoil fold from the mushroom Coprinopsis cinerea, named cocaprins, which inhibit both cysteine and aspartic proteases. Two cocaprin-encoding genes are differentially expressed in fungal tissues. One is highly transcribed in vegetative mycelium and the other in the stipes of mature fruiting bodies. Cocaprins are small proteins (15 kDa) with acidic isoelectric points that form dimers. The three-dimensional structure of cocaprin 1 showed similarity to fungal β-trefoil lectins. Cocaprins inhibit plant C1 family cysteine proteases with Ki in the micromolar range, but do not inhibit the C13 family protease legumain, which distinguishes them from mycocypins. Cocaprins also inhibit the aspartic protease pepsin with Ki in the low micromolar range. Mutagenesis revealed that the β2-β3 loop is involved in the inhibition of cysteine proteases and that the inhibitory reactive sites for aspartic and cysteine proteases are located at different positions on the protein. Their biological function is thought to be the regulation of endogenous proteolytic activities or in defense against fungal antagonists. Cocaprins are the first characterized aspartic protease inhibitors with β-trefoil fold from fungi, and demonstrate the incredible plasticity of loop functionalization in fungal proteins with β-trefoil fold.

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Correction: Plasticity of the β-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence System

Cited by 4 publications

References 0 publications

Dimerization of the fungal defense lectin CCL2 is essential for its toxicity against nematodes

Dimerization of the fungal defense lectin CCL2 is essential for its toxicity against nematodes

Transcriptomic atlas of mushroom development highlights an independent origin of complex multicellularity

Cocaprins, β-Trefoil Fold Inhibitors of Cysteine and Aspartic Proteases from Coprinopsis cinerea

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