Structure of a lectin with antitumoral properties in king bolete (Boletus edulis) mushrooms

A novel lectin has been isolated from the fruiting bodies of the common edible mushroom Boletus edulis (king bolete, penny bun, porcino or cep) by affinity chromatography on a chitin column. We propose for the lectin the name BEL (B. edulis lectin). BEL inhibits selectively the proliferation of seve...

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Bibliographic Details
Published in:Glycobiology (Oxford) 2011-08, Vol.21 (8), p.1000-1009
Main Authors: Bovi, Michele, Carrizo, Maria E, Capaldi, Stefano, Perduca, Massimiliano, Chiarelli, Laurent R, Galliano, Monica, Monaco, Hugo L
Format: Article
Language:English
Subjects:
Agaricales - chemistry
Agaricus bisporus
Amino Acid Sequence
Antineoplastic Agents - chemistry
Antineoplastic Agents - isolation & purification
Antineoplastic Agents - pharmacology
Boletus
Cell Line, Tumor
Cell Proliferation - drug effects
Chromatography, Affinity
Crystallography, X-Ray
Dose-Response Relationship, Drug
Drug Screening Assays, Antitumor
Fruiting Bodies, Fungal - chemistry
Humans
Lectins - chemistry
Lectins - isolation & purification
Lectins - pharmacology
Models, Molecular
Protein Conformation
Sequence Alignment
Structure-Activity Relationship
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Summary:A novel lectin has been isolated from the fruiting bodies of the common edible mushroom Boletus edulis (king bolete, penny bun, porcino or cep) by affinity chromatography on a chitin column. We propose for the lectin the name BEL (B. edulis lectin). BEL inhibits selectively the proliferation of several malignant cell lines and binds the neoplastic cell-specific T-antigen disaccharide, Gal 1-3GalNAc. The lectin was structurally characterized: the molecule is a homotetramer and the 142-amino acid sequence of the chains was determined. The protein belongs to the saline-soluble family of mushroom fruiting body-specific lectins. BEL was also crystallized and its three-dimensional structure was determined by X-ray diffraction to 1.15 Å resolution. The structure is similar to that of Agaricus bisporus lectin. Using the appropriate co-crystals, the interactions of BEL with specific mono- and disaccharides were also studied by X-ray diffraction. The six structures of carbohydrate complexes reported here provide details of the interactions of the ligands with the lectin and shed light on the selectivity of the two distinct binding sites present in each protomer.
ISSN:0959-6658
1460-2423
DOI:10.1093/glycob/cwr012