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

BOVI, MICHELE; CARRIZO, MARÍA E.; CAPALDI, STEFANO; PERDUCA, MASSIMILIANO; CHIARELLI, LAURENT; GALLIANO, MONICA; MONACO, HUGO L.

OXFORD UNIV PRESS INC

Año: 2011 vol. 21 p. 1000 - 1000

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 (Boletus edulis lectin). BEL inhibits selectively the proliferation of several malignant cell lines and binds the neoplastic cell specific T-antigen disaccharide, Galbeta1-3GalNAc. 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 comple