| Summary: | <i>Mycobacterium tuberculosis</i> (<i>M.tb</i>)-encoded factors protect it against host-generated stresses and support its survival in the hostile host environment. <i>M.tb</i> possesses two peptidyl-prolyl <i>cis-trans</i> isomerases and a probable trigger factor encoded by <i>Rv2462c</i> which has an FKBP-like PPIase domain. PPIases are known to assist the folding of peptidyl-prolyl bonds and are involved in various cellular processes important for bacterial survival in host-generated stresses. In this study, we aim to functionally characterize <i>Rv2462c</i> of <i>M.tb.</i> Our data suggest that the trigger factor of <i>M.tb</i> exhibits chaperone activity both in vitro and in vivo. Heterologous expression of <i>M.tb</i>-<i>Rv2462c</i> locus into <i>Mycobacterium smegmatis</i> enhanced its survival within macrophages, adaptation to oxidative stress and biofilm formation. <i>M.tb</i>-trigger factor has strong immunomodulatory potential and modifies the cytokine profile of the host towards the proinflammatory axis.
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