In Silico Characterization of Glutathione-S-transferase from Genus Trichinella

Abstract

Glutathione-S-transferase is a major immunomodulator and belongs to the family of multifunctional enzymes which involves in the various detoxification processes in the nematodes. There are various kinds of membrane-bound glutathione-S-transferases are present and involved in xenobiotic metabolism processes. Glutathione-S-transferases have shown promising properties of a potential target molecule to control the population of Trichinella species which is the causative agent of trichinosis. In silico prediction of gene and proteins is of great importance for structural and functional characterization of genomic and proteomic sequences. In the present investigations, 07 sequences of Glutathione-S transferase of nematodes from the various species of genus Trichinella were characterized. In silco analysis of Glutathione-S-transferase proteins like their amino acid compositions, atomic composition, the extinction coefficient of protein along with estimated half-life, instability index of protein, aliphatic index and grand average of hydropathicity were also analyzed. Physicochemical properties, secondary and tertiary structural details of proteins with their relationship with each other will help researchers to design a synthetic drug against Trichinellosis. These results may provide theoretical grounds for future studies of nematode vaccine development.