Work

Characterization of inositol phospho-sphingolipid-phospholipase C 1 (Isc1) inCryptococcus neoformansreveals unique biochemical features

Year: 2011

Type: article

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.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2011.01.015

Authors: Jennifer Henry, Aimee Guillotte, Chiara Luberto, Maurizio Del Poeta

Institution: Medical University of South Carolina

Language: English

Topic: Fungal Infections and Studies

Subfield: Epidemiology

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of Allergy and Infectious Diseases, National Center for Research Resources