| Literature DB >> 21256847 |
Jennifer Henry1, Aimee Guillotte, Chiara Luberto, Maurizio Del Poeta.
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.Entities:
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Year: 2011 PMID: 21256847 PMCID: PMC3045780 DOI: 10.1016/j.febslet.2011.01.015
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124