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Lectins are non-immunoglobulin carbohydrate-binding proteins without enzymatic activity towards the bound carbohydrates. Many lectins of e.g. plants or fungi have been suggested to act as toxins to defend the host against predators and parasites. We have previously shown that the  Coprinopsis cinerea  lectin 2 (CCL2), which binds to α1,3-fucosylated N-glycan cores, is toxic to  Caenorhabditis elegans  and results in developmental delay and premature death. In this study, we investigated the underlying toxicity phenotype at the cellular level by electron and confocal microscopy. We found that CCL2 directly binds to the intestinal apical surface and leads to a highly damaged brush border with loss of microvilli, actin filament depolymerization, and invaginations of the intestinal apical plasma membrane through gaps in the terminal web. We excluded several possible toxicity mechanisms such as internalization and pore-formation, suggesting that CCL2 acts directly on intestinal apical plasma membrane or glycocalyx proteins. A genetic screen for  C .  elegans  mutants resistant to CCL2 generated over a dozen new alleles in  bre 1 ,  ger 1 , and  fut 1 , three genes required for the synthesis of the sugar moiety recognized by CCL2. CCL2-induced intestinal brush border defects in  C .  elegans  are similar to the damage observed previously in rats after feeding the dietary lectins wheat germ agglutinin or concanavalin A. The evolutionary conserved reaction of the brush border between mammals and nematodes might allow  C .  elegans  to be exploited as model organism for the study of dietary lectin-induced intestinal pathology in mammals.

Disruption of the C. elegans Intestinal Brush Border by the Fungal Lectin CCL2 Phenocopies Dietary Lectin Toxicity in Mammals