RNA-seq data of the Amphotericin (AmB)-resistant Aspergillus strain 211 and its AmB-susceptible sectorized derivative with and without AmB treatment
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ABSTRACT:
PROVIDER: PRJNA1163339 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR30735500_1.fastq.gz | Fastqsanger.gz | |||
| SRR30735500_2.fastq.gz | Fastqsanger.gz | |||
| SRR30735501_1.fastq.gz | Fastqsanger.gz | |||
| SRR30735501_2.fastq.gz | Fastqsanger.gz | |||
| SRR30735502_1.fastq.gz | Fastqsanger.gz |
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Project description:Amphotericin B (AMB) is the most widely used polyene antifungal drug for the treatment of systemic fungal infections including invasive aspergillosis. We aimed to understand molecular targets of AMB in Aspergillus fumigatus (Afu) by genomic approaches. Amphotericin B (AMB) is the most widely used polyene antifungal drug for the treatment of systemic fungal infections including invasive aspergillosis. We aimed to understand molecular targets of AMB in Aspergillus fumigatus (Afu) by microarray and proteomic methods. Keywords: Aspergillus fumigatus treated with amphotericin B for 24 hours Experiment was performed in dye swap manner from two different biological replicates
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Project description:The filamentous fungus Aspergillus fumigatus is an opportunistic human pathogen, which can cause mycoses and allergies in susceptible individuals. With regard to therapy, the polyene drug amphotericin B (AmB) is still frequently used to treat Aspergillus fumigatus infections due to the fact that it remains effective against azole-resistant Aspergillus strains. AmB binds to ergosterol in the fungal membrane, but its mode of action and the fungal resistance mechanisms involved have not been completely elucidated yet. To get further insights into the drug mechanisms of AmB, we investigated the proteomic profile of A. fumigatus in response to AmB and its liposomal formulation by LC-MS/MS analysis. A significant increase (≥ 2-fold) in abundance of 202 different proteins in response to AmB and 193 in case of liposomal AmB was observed, while the level of 70 and 83 proteins decreased, respectively. In particular, the level of proteins anchored to the membrane, involved in catabolic processes, aromatic acid degradation, or secondary metabolism increased prominently. Of particular note was the more than 300-fold increase of a RTA1 domain-containing protein after AmB treatment. Fungal RTA-like proteins represent lipid-translocating exporters, which are characterized by multiple transmembrane regions and often confer resistance to toxic chemicals. Indeed, the deletion of the corresponding gene in A. fumigatus led to an increased susceptibility to AmB and other antifungal polyenes such as nystatin. Particularly worthy of mention is that some of the most significantly increased proteins included enzymes involved in the biosynthesis of secondary metabolites such as the prenylated polyphenol fumicycline as well as xanthocillin and hexadehydro-astechrome, which both form complexes with transition metals.
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