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• W2904420586 abstract "Heat shock protein 90 is one of the most abundant and evolutionary conserved class of molecular chaperones present throughout the biological kingdom. It is a specialist chaperone as its function extends beyond protein homeostasis. It is known to chaperone a specific set of proteins which lies at the interface of important cellular processes such as growth, signal transduction and developmental networks. It is believed that Hsp90 also functions as a stress responsive storehouse of genetic variation and thereby plays a key role in evolution. Another novel facet of Hsp90 was uncovered when the function of this chaperone was found to be important for pathogenesis of infectious disease-causing agents. Hsp90 was found to regulate stage transition in clinically important protozoan parasites such as Plasmodium, Giardia, Entamoeba and Leishmania. Fungal pathogens cause substantial morbidity and mortality worldwide, however, the true impact of this group of pathogens on human health is not widely appreciated. Majority of fungal infections are often concealed under major comorbid conditions such as AIDS, cancer and other immunosuppressive conditions. Diagnosis and treatment of fungal infections is notoriously challenging due to emerging pathogens and drug resistance. Prospects of targeting Hsp90 to curb fungal pathogens has been explored in Candida albicans and Aspergillus fumigatus. Studies have revealed that Hsp90 governs one of the classical virulence traits of C. albicans, the yeast to hyphal transition. Additionally, the role of Hsp90 in potentiating antifungal resistance has been examined by genetic and inhibitor based studies. In this study, I have explored novel facets of Hsp90 in two clinically important fungal pathogens: Candida and Cryptococcus. Candida and Cryptococcus are the among the chief cause of death in cancer and AIDS patients. Furthermore, there is a surge in nosocomial fungal infections worldwide. I have investigated the hierarchy of Candida species implicated in invasive infections and found a clinical misdiagnosis of a multidrug resistant pathogen, Candida auris. Further, I have explored the role of Hsp90 in aiding resistance and thermotolerance of this emerging fungal pathogen.Comparative analysis of Hsp90s of Candida and Cryptococcus As mentioned previously, despite the great interest in examining the potential of Hsp90 to serve as a drug target to treat fungal infections, the basic biochemical properties of Hsp90s from fungal pathogens have not been studied previously. With this view, in Chapter 3, I have compared the biochemical properties of Hsp90 of these two fungal pathogens. Functionally, Hsp90 is an ATPase and the N-terminal domain of the protein harbours the nucleotide binding pocket. ATP hydrolysis is essential for its chaperoning ability. Bioinformatic analysis of the binding pocket of both Candida Hsp90 (CaHsp90) and Cryptococcus Hsp90 (CnHsp90) revealed subtle differences in the amino acid residues implicated in ATP binding, despite general conservation at the level of its primary…" @default.
• W2904420586 created "2018-12-22" @default.
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• W2904420586 date "2018-11-06" @default.
• W2904420586 modified "2023-09-24" @default.
• W2904420586 title "Understanding the Biology of Heat Shock Protein 90 in Opportunistic Fungal Pathogens" @default.
• W2904420586 hasPublicationYear "2018" @default.
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