Small but powerful: The role of HSP in bacterial infectious disease pathogenesis- A mini-review of recent findings

Abstract

Heat Shock Proteins (Hsp) are evolutionarily conserved ubiquitous molecular chaperones usually produced when cells are exposed to temperatures beyond their normal growth temperature. They are a group of ATP-independent chaperons pivotal for cell survival and proliferation. This group of proteins has been well studied over the years. However, recent investigations leveraging the available Whole Genome Sequencing (WGS) approach are beginning to shed more light on how this protein interacts with other intracellular proteins to modulate bacterial virulence and pathogenesis. Bacteria cells that manufacture HSPs can survive at higher temperatures. Certain heat-shock proteins have a refolding or degradation action that can save the bacterial cell even in extreme stress demands and even help some bacteria transition from being commensal to a pathogen. Certain HSPs are virulence factors, while others modulate bacterial pathogenesis increasing bacterial resistance to host immunological attack. Interestingly, others also influence certain virulence gene expressions. Several mechanisms govern heat shock response. Moreover, the employment of specific regulatory proteins that exert a positive or negative effect on the initiation of transcription by the RNA polymerase enzyme is successful and efficient in controlling heat-shock gene transcription. Interestingly, most pathogens use several approaches to reprogram gene transcription in response to diverse stress rapidly. In this mini-review, we tactfully discussed the recent update on HSP in bacteria virulence and how these proteins could serve as potential drug targets. Moreover, we provided an overview of how HSPs are regulated in bacterial pathogens favouring bacterial survival in diverse cellular niches.