Heat shock proteins in the pathogenesis of mycobacterium tuberculosis

Abstract

Mycobacterium tuberculosis (M. tb), the causative agent of tuberculosis, is responsible for immense global suffering taking nearly 1.5 million lives annually (WHO 2016). About one-third of the world’s population is estimated to be infected with this obligate pathogen and yet remains asymptomatic (Raviglione and Sulis 2016). M. tb is highly adapted for survival in the extremely hostile intracellular environment in host macrophages. The ability of M. tb to overcome various host-induced proteotoxic stress conditions relies significantly on its highly efficient chaperone network. Heat shock proteins (Hsps) form a special class of the chaperone network and exhibit an orchestrated repertoire of stresssensing mechanisms. Hsps, found ubiquitously in most prokaryotes as well as eukaryotes, are very well conserved across the species. In this chapter, we discuss about the recent advances in understanding the myriad number of molecular pathways that Hsps regulate, directly or otherwise in M. tb, which highlight the association between Hsps and virulence determination in Mycobacterium.