Characterization of inositol phospho-sphingolipid-phospholipase C 1 (Isc1) in Cryptococcus neoformans reveals unique biochemical features |
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| Authors: | Henry Jennifer Guillotte Aimee Luberto Chiara Del Poeta Maurizio |
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| Affiliation: | aDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA;bDepartment of Microbiology and Immunology, Medical University of South Carolina, Charleston, SC, USA;cDepartment of Craniofacial Biology, Medical University of South Carolina, Charleston, SC, USA;dDivision of Infectious Diseases, Medical University of South Carolina, Charleston, SC, USA |
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| Abstract: | In this work, we biochemically characterized inositol phosphosphingolipid-phospholipase C (Isc1) from the pathogenic fungus Cryptococcus neoformans. Unlike Isc1 from other fungi and parasites which hydrolyze both fungal complex sphingolipids (IPC-PLC) and mammalian sphingomyelin (SM-PLC), C. neoformans Isc1 only exerts IPC-PLC activity. Genetic mutations thought to regulate substrate recognition in other Isc1 proteins do not restore SM-PLC activity of the cryptococcal enzyme. C. neoformans Isc1 regulates the level of complex sphingolipids and certain species of phytoceramide, especially when fungal cells are exposed to acidic stress. Since growth in acidic environments is required for C. neoformans to cause disease, this study has important implications for understanding of C. neoformans pathogenicity. |
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| Keywords: | Phospholipase C Inositol sphingolipids Sphingomyelin Phytoceramide Plasma membrane ATPase Cryptococcus neoformans |
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