Abstract
The heat shock proteins (HSPs) function as chaperones to facilitate proper folding and modification of proteins and are of particular importance when organisms are subjected to unfavourable conditions. The human fungal pathogens are subjected to such conditions within the context of infection as they are exposed to human body temperature as well as the host immune response. Herein, the roles of the major classes of HSPs are briefly reviewed and their known contributions in human fungal pathogens are described with a focus on Candida albicans, Cryptococcus neoformans, and Aspergillus fumigatus. The Hsp90s and Hsp70s in human fungal pathogens broadly contribute to thermotolerance, morphological changes required for virulence, and tolerance to antifungal drugs. There are also examples of J domain co-chaperones and small HSPs influencing the elaboration of virulence factors in human fungal pathogens. However, there are diverse members in these groups of chaperones and there is still much to be uncovered about their contributions to pathogenesis. These HSPs do not act in isolation, but rather they form a network with one another. Interactions between chaperones define their specific roles and enhance their protein folding capabilities. Recent efforts to characterize these HSP networks in human fungal pathogens have revealed that there are unique interactions relevant to these pathogens, particularly under stress conditions. The chaperone networks in the fungal pathogens are also emerging as key coordinators of pathogenesis and antifungal drug tolerance, suggesting that their disruption is a promising strategy for the development of antifungal therapy.
Highlights
Human fungal pathogens must be able to survive and proliferate in the host environment despite several unfavourable conditions
In order to survive at core human body temperature and to undergo these morphological changes, fungi must be able to cope with the proteotoxic stress induced at high temperature and upon flux in the demand for protein production
The sumoylation of Hsp104 contributes to the thermotolerance to heat shock at 42 ◦ C of C. albicans [82]. The roles of these chaperones have not been characterized in other fungi, Hsp104 is required for the acquisition of thermotolerance in S. cerevisiae [79] suggesting that it could potentially contribute to fungal adaptation to a mammalian host
Summary
Human fungal pathogens must be able to survive and proliferate in the host environment despite several unfavourable conditions. De novo, stabilizing protein conformation under stress conditions, and modulating proThe HSPs are involved in multiple processes including folding proteins de novo, stabilizing tein conformation to regulate their activity [7]. Energy-dependent and -independent chaperones aschaperones well as theiras well as their co-chaperones coordinately ensure that cells can function in and co-chaperones coordinately ensure that cells can function in normal and stressednormal conditions stressed conditions including those relevant to proliferation a human host. The major including those relevant to proliferation in a human host. Fungi 2021, 7, 209 to wild type or untreated strains (red line)
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