Expression, purification, characterization, and cytotoxic evaluation of the ML1-STxB fusion protein in E. coli

Abstract

Abstract One of the newest treatment options for cancer is the targeted delivery of the toxin substance to the cancer cells. These toxins should contain different moieties for finding and killing cancer cells. One of these toxins in Mistletoe ML1 protein is an inactive ribosomal protein and can be considered as an anticancer agent. Therefore, it seems that by fusion of ML1 protein with another protein called Shiga toxin B (STxB), which can bind to Gb3 (Globotriosyl Ceramide) receptor that is abundantly expressed on the cancer cells, a recombinant protein with selective permeability may be produced in cancer cells. In the current study, we aimed to produce and purify a fusion protein containing ML1 as a toxic moiety fused to STxB, targeting moiety, and assessing its cytotoxic activities.