Abstract

Tuberculosis (TB) is currently among the major ten causes for death worldwide being brought about 1.7 million passing in 2016. The singular vaccine candidate available for its treatment till now is Bacillus Calmette-Guerin (BCG) which now also fails to provide accurate protection against this deadly disease. Mycobacterium tuberculosis H₃₇Rv (M. tuberculosis H₃₇Rv), the causative agent of this malady is currently turned out to be so intense and make extremely difficult to treat its infection. This manuscript covers some bioinformatics approaches against conserved hypothetical proteins which pretend to act as a thioredoxin-like protein. Thioredoxin (Trx) proteins are the redox proteins that are rotate between two forms, one is oxidized disulfide and the other one is reduced dithiol forms. Therefore it is said to be as an important component in many cellular redox reactions. The Trx protein of our study contains a conserved motif CXXC which is essential for its enzymatic activity. Mutational analysis of this protein declares its essentiality instability of the protein. This study concludes that this protein might be essential in several cellular processes carried out by this bacterium and further targeting this protein might give us a novel therapeutic antituberculosis drug.

Keywords: Mycobacterium tuberculosis H₃₇Rv; Alveolar macrophages; Phagolysosome; Thioredoxin; Cysteine