Drug targets identification of Mycobacterium tuberculosis by metabolic pathway analysis: insilico process
Tuberculosis (TB) has been declared as a global health emergency by the World Health Organization(WHO). This has been mainly due to the emergence of multiple drug resistant strains and the synergy between tubercle bacilli and the human immunodeficiency virus (HIV). Mycobacterium tuberculosis (Mtb) is a pathogenic bacteria species in the genus Mycobacterium and the causative agent of most cases of tuberculosis. Tuberculosis (TB) is the leading cause of death in the world from a bacterial infectious disease. This antibiotic resistance strain lead to development of the new antibiotics or drug molecules which can kill or suppress the growth of Mycobacterium tuberculosis.The need for new antiTB is persistent due to the emergence of drug resistant Mycobacterium tuberculosis. Here we aimto identify new drug targets in Mycobacterium tuberculosis by phylogenomics among the Mycobacterium tuberculosisandcomparative genomics to Homo sapiens. The proposed target discovery pipeline is largely independent of experimental data and based on the assumption that Mycobacterium tuberculosis proteins are likely to be essential if (i) there are no similar proteins in the same proteome and (ii) they are highly conserved across the Mycobacterium tuberculosisof mammals. We have performed an in silicocomparative analysis of metabolic pathways of the host Homo sapiens and the pathogen Mycobacterium tuberculosis (H37Rv). Novel efforts in developing drugs that target the intracellular metabolismof M. tuberculosis often focus on metabolic pathways that are specific to M. tuberculosis. We have identified five unique pathwaysfor Mycobacterium tuberculosis having a number of 60 enzymes, which are nonhomologous to Homo sapiens protein sequences,and among them there were 55 enzymes, which are nonhomologous to Homo sapiens protein sequences.These enzymes were alsofound to be essential for survival of theMycobacteriumtuberculosisaccording to the DEG database. Further, the functional analysis using Uniprot showed involvement of all the unique enzymes in the different cellular components.