Abstract
BACKGROUND: Developing safe drugs for tuberculosis (TB), is a major challenge due to upsurge in drug resistance, hepatotoxicity, and the presence of Mycobacterium tuberculosis (Mtb) targets orthologs in human and its non-pathogenic host E. coli. Prostaglandin G/H synthase-2 and 30S ribosomal-S12 protein of Mtb show 100 and 48% similarity with human proteins respectively. Thus, targeting these Mtb proteins by p-aminosalicylic acid and streptomycin for the treatment of TB adversely affect human metabolism, and warrants to identify novel and unique drug targets of Mtb.
METHODS: In the present study, in-silico study has been performed to find novel and unique drug targets of Mtb H37Rv.
RESULTS : We report ten unique target proteins of Mtb, which do not possess any similarity with human/non-pathogenic E. coli proteins. Out of 3,993 retrieved proteins of Mtb H37Rv, a total of 1596 and 913 proteins unique to Mtb were identified by comparing with human and E. coli proteome, respectively. Further comparison of 1596 and 913 proteins led to the identification of 515 (out of which, 230 are functionally known) unique proteins of Mtb that are absent in both humans and E. coli.
CONCLUSIONS: Gene ontology (GO) analysis of these 230 proteins finally led to the recognition of 10 proteins participated in the various biological processes of Mtb that may serve as potential novel antitubercular drug targets.