Jerica Sabotič (Author), Janko Kos (Author)

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, against both invertebrates and cancer-derived cell lines. In addition, CNL exhibits potent immunostimulation of human dendritic cells, resulting in a strong T helper cell type 1 response. Based on its unique characteristics, CNL is a promising candidate for applications in human and veterinary medicine as well as in agriculture, for plant protection.

Keywords

beta-trefoil fold;LacDiNAc;entomotoxic;leukemic T-cell;antiproliferative;dendritic cell;

Data

Language: English
Year of publishing:
Typology: 1.02 - Review Article
Organization: UL FFA - Faculty of Pharmacy
UDC: 577
COBISS: 32898599 Link will open in a new window
ISSN: 1420-3049
Views: 239
Downloads: 60
Average score: 0 (0 votes)
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Other data

Type (COBISS): Article
Pages: str. 4204--4204-10
Volume: ǂVol. ǂ24
Issue: ǂno. ǂ23
Chronology: 2109
DOI: 10.3390/molecules24234204
ID: 13918251