Homology modeling analysis of the effect of α and β subunits of the interaction of Shiga toxin with Interferon gamma, Prostaglandin G/H synthase 2, and Sodium/ glucose cotransporter 1 proteins as a step for cancer suppression

With of bioinformatics technology advancement, new methods of cancer treatment, such as the use of bacterial toxins, can now be explored more rapidly. In the present bioinformatics study, the probable attachment of Shiga toxin subunits to Interferon gamma (IFNG), Prostaglandin G/H synthase 2 (PTGS2), and Sodium/ glucose cotransporter 1 (SGLT1) was investigated to take a step towards cancer suppression.

The gene sequences were extracted from NCBI database. SWISS-MODE and jmol databases were used to detect the sequence and model the three-dimensional structure of proteins, respectively. The effect of StxA and StxB on IFNG, PTGS2 and SGLT1 proteins was evaluated with ZDOCK data base.

Three-dimensional structure of proteins showed that the StxA protein was not a monomer, and that StxB had flat structures that bound it to the cell surface. Alpha helices and beta sheets are present in IFNG, and this monomeric protein lacks a symmetric tertiary structure. PTGS2 has a large complex structure consisting of several alpha helices and a beta sheet. In SGLT1, which is a transmembrane protein, only alpha helices were seen. There is a significant interaction between Shiga toxin protein and all three proteins IFNG, PTGS2 and SGLT1 by the method of molecular docking.

Findings of this study provide a new dedication for laboratory studies of the effect of Shiga toxin to evaluate its ability to stimulate the immune system, reduce tumor growth and treat cancer according to its ability to attach to the proteins which are effective in these processes.