Aspergillus fumigatus alb1 encodes naphthopyrone synthase when expressed in Aspergillus oryzae
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منابع مشابه
Capsule Polysaccharide Synthase 1 (CPS1) Homolog in Aspergillus fumigatus: A Gene Disruption Study
Introduction: Aspergillus fumigatus is the leading cause of invasive aspergillosis in immunocompromised patients with a high rate of mortality. Despite introduction of several classes of antifungal drugs, the limitations of current therapies have prompted an intense research toward the discovery of new antifungal compounds. In a recent study, several potential drug targets were identified based...
متن کاملRole of laeA in the Regulation of alb1, gliP, Conidial Morphology, and Virulence in Aspergillus fumigatus.
The alb1 (pksP) gene has been reported as a virulence factor controlling the pigmentation and morphology of conidia in Aspergillus fumigatus. A recent report suggested that laeA regulates alb1 expression and conidial morphology but not pigmentation in the A. fumigatus strain AF293. laeA has also been reported to regulate the synthesis of secondary metabolites, such as gliotoxin. We compared the...
متن کاملAspergillus fumigatus in Poultry
Aspergillus fumigatus remains a major respiratory pathogen in birds. In poultry, infection by A. fumigatus may induce significant economic losses particularly in turkey production. A. fumigatus develops and sporulates easily in poor quality bedding or contaminated feedstuffs in indoor farm environments. Inadequate ventilation and dusty conditions increase the risk of bird exposure to aerosolize...
متن کاملGlycosylinositolphosphoceramides in Aspergillus fumigatus.
Fungal glycosylinositolphosphoceramides (GIPCs) are involved in cell growth and fungal-host interactions. In this study, six GIPCs from the mycelium of the human pathogen Aspergillus fumigatus were purified and characterized using Q-TOF mass spectrometry and 1H, 13C, and 31P NMR. All structures have the same inositolphosphoceramide moiety with the presence of a C(18:0)-phytosphingosine conjugat...
متن کاملCharacterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli.
To characterize aspartyl aminopeptidase from Aspergillus oryzae, the recombinant enzyme was expressed in Escherichia coli. The enzyme cleaves N-terminal acidic amino acids. About 30% activity was retained in 20% NaCl. Digestion of defatted soybean by the enzyme resulted in an increase in the glutamic acid content, suggesting that the enzyme is potentially responsible for the release of glutamic...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 2000
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.2000.tb09356.x