Purification and characterization of a novel protein with activity against non-small-cell lung cancer in vitro and in vivo from the edible mushroom Boletus edulis

A new anti-tumor protein (designated as Boletus edulis or in short BEAP) was isolated from dried fruit bodies of the edible bolete mushroom Boletus edulis. The purification protocol employed comprised fast ion exchange chromatography on a Hitrap Q column and ion exchange chromatography on a DEAE-52 cellulose column. Superdex G75 gel filtration and SDS-PAGE analysis revealed that BEAP was a protein with a molecular weight of 16.7 KD. The protein exhibited potent anti-cancer activity on A549 cells both in vitro and in vivo. With the use of AO/EB staining, annexin V-FITC/P1. and Western blotting, it was demonstrated in vitro that the cytotoxicity of BEAP was mediated by induction of apoptosis and arrest of A549 cells in the G1 phase of the cell cyde. BEAP significantly suppressed the growth of A549 solid tumors in vivo. These results prove that BEAP is a new multifunctional protein with anti-tumor and anti-metastasis capabilities. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

A new anti-tumor protein BEAP was isolated from the dried fruit bodies of the edible bolete mushroom Boletus edulis. This protein exhibited potent anti-cancer activity on A549 cells both in vitro and in vivo, mediating cytotoxicity through induction of apoptosis and cell cycle arrest in the G1 phase. BEAP also significantly suppressed the growth of A549 solid tumors in vivo, demonstrating its multifunctional anti-tumor and anti-metastasis capabilities.