Characterization of inositol phospho-sphingolipid-phospholipase C 1 (Isc1) in Cryptococcus neoformans reveals unique biochemical features

Jennifer Henry; Aimee Guillotte; Chiara Luberto; Maurizio Del Poeta

doi:10.1016/j.febslet.2011.01.015

Characterization of inositol phospho-sphingolipid-phospholipase C 1 (Isc1) in Cryptococcus neoformans reveals unique biochemical features

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

Medical University of South Carolina

Research output: Contribution to journal › Article › peer-review

30 Scopus citations

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.

Original language	English
Pages (from-to)	635-640
Number of pages	6
Journal	FEBS Letters
Volume	585
Issue number	4
DOIs	https://doi.org/10.1016/j.febslet.2011.01.015
State	Published - Feb 18 2011

Keywords

Cryptococcus neoformans
Inositol sphingolipids
Phospholipase C
Phytoceramide
Plasma membrane ATPase
Sphingomyelin

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10.1016/j.febslet.2011.01.015

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title = "Characterization of inositol phospho-sphingolipid-phospholipase C 1 (Isc1) in Cryptococcus neoformans reveals unique biochemical features",

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.",

keywords = "Cryptococcus neoformans, Inositol sphingolipids, Phospholipase C, Phytoceramide, Plasma membrane ATPase, Sphingomyelin",

author = "Jennifer Henry and Aimee Guillotte and Chiara Luberto and \{Del Poeta\}, Maurizio",

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AU - Henry, Jennifer

AU - Guillotte, Aimee

AU - Luberto, Chiara

AU - Del Poeta, Maurizio

PY - 2011/2/18

Y1 - 2011/2/18

N2 - 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.

AB - 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.

KW - Cryptococcus neoformans

KW - Inositol sphingolipids

KW - Phospholipase C

KW - Phytoceramide

KW - Plasma membrane ATPase

KW - Sphingomyelin

UR - https://www.scopus.com/pages/publications/79951581102

U2 - 10.1016/j.febslet.2011.01.015

DO - 10.1016/j.febslet.2011.01.015

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AN - SCOPUS:79951581102

SN - 0014-5793

VL - 585

SP - 635

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JO - FEBS Letters

JF - FEBS Letters

IS - 4

ER -

Characterization of inositol phospho-sphingolipid-phospholipase C 1 (Isc1) in Cryptococcus neoformans reveals unique biochemical features

Abstract

Keywords

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