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Characterization of inositol phospho‐sphingolipid‐phospholipase C 1 (Isc1) in Cryptococcus neoformans reveals unique biochemical features
Author(s) -
Henry Jennifer,
Guillotte Aimee,
Luberto Chiara,
Del Poeta Maurizio
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.01.015
Subject(s) - cryptococcus neoformans , sphingolipid , sphingomyelin , biology , inositol , phospholipase , biochemistry , phospholipase c , microbiology and biotechnology , virulence , enzyme , pathogenic fungus , ceramide , sphingosine , gene , cholesterol , receptor , apoptosis
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.