Neutral glycolipids of the filamentous fungus Neurospora crassa: altered expression in plant defensin-resistant mutants.
J Lipid Res
; 46(4): 759-68, 2005 Apr.
Article
en En
| MEDLINE
| ID: mdl-15654124
ABSTRACT
To defend themselves against fungal pathogens, plants produce numerous antifungal proteins and peptides, including defensins, some of which have been proposed to interact with fungal cell surface glycosphingolipid components. Although not known as a phytopathogen, the filamentous fungus Neurospora crassa possesses numerous genes similar to those required for plant pathogenesis identified in fungal pathogens (Galagan, J. E., et al. 2003. Nature 422 859-868), and it has been used as a model for studying plant-phytopathogen interactions targeting fungal membrane components (Thevissen, K., et al. 2003. Peptides. 24 1705-1712). For this study, neutral glycolipid components were extracted from wild-type and plant defensin-resistant mutant strains of N. crassa. The structures of purified components were elucidated by NMR spectroscopy and mass spectrometry. Neutral glycosphingolipids of both wild-type and mutant strains were characterized as beta-glucopyranosylceramides, but those of the mutants were found with structurally altered ceramides. Although the wild type expressed a preponderance of N-2'-hydroxy-(E)-Delta3-octadecenoate as the fatty-N-acyl component attached to the long-chain base (4E,8E)-9-methyl-4,8-sphingadienine, the mutant ceramides were found with mainly N-2'-hydroxyhexadecanoate instead. In addition, the mutant strains expressed highly increased levels of a sterol glucoside identified as ergosterol-beta-glucoside. The potential implications of these findings with respect to defensin resistance in the N. crassa mutants are discussed.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas de Plantas
/
Glucolípidos
/
Defensinas
/
Farmacorresistencia Fúngica
/
Mutación
/
Neurospora crassa
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
J Lipid Res
Año:
2005
Tipo del documento:
Article
País de afiliación:
Estados Unidos