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CNL-Clitocybe nebularis Lectin-The Fungal GalNAcβ1-4GlcNAc-Binding Lectin.


ABSTRACT: Clitocybe nebularis lectin (CNL) is present in fruiting bodies of clouded agaric along with several similar isolectins that are all small and stable proteins. It is a beta-trefoil type lectin forming homodimers that are essential for its functionality. It binds specifically N,N'-diacetyllactosediamine (GalNAcβ1-4GlcNAc, LacDiNac) and human blood group A determinant-containing glycan epitopes. Its most probable function is to defend fruiting bodies against predators and parasites. In addition, an endogenous regulatory function is possible for CNL, as indicated by its interaction with fungal protease inhibitors sharing the beta-trefoil fold. CNL is toxic to insects, nematodes and amoebae, as well as to leukemic T-cell lines. Bivalent carbohydrate binding is essential for the toxicity of CNL,

SUBMITTER: Sabotic J 

PROVIDER: S-EPMC6930499 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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