Heterologous expression and characterization of a new galactose-binding lectin from Bauhinia forficata with antiproliferative activity.

In this study, we describe the characterization of a new lectin, BfL-II, purified from the seeds of Bauhinia forficata, which is distinct, at sequence-level, from the previously reported lectin from the same specie (BfL). In addition, the gene for this lectin was cloned and expressed in Escherichia coli and its antiproliferative activity was evaluated against human breast and colorectal cancer cells (MCF-7 and HT-29, respectively). The treatment with 100 µg/µL of either native or recombinant BfL (nBfL or rBfL) significantly reduced the proliferation of both cancer cell lines (p < 0.01). The inhibition of HT-29 cell proliferation was as high as 82.5% and 93.6% with 100 µg/µL of rBfL-I and nBfL after 24 h, respectively. Therefore, BfL-II presents a promising antiproliferative activity, which may be applied in the development of new anticancer treatments.