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Evolution of antifungal drug resistance in Candida albicans.

ABSTRACT: Unravelling the role of mistranslation in the acquisition of drug tolerance and resistance in Candida albicans.

PROVIDER: PRJEB46537 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ERR6565670_1.fastq.gz	Fastqsanger.gz
	ERR6565670_2.fastq.gz	Fastqsanger.gz
	ERR6565671_1.fastq.gz	Fastqsanger.gz
	ERR6565671_2.fastq.gz	Fastqsanger.gz
	ERR6565669_1.fastq.gz	Fastqsanger.gz

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Mistranslation accelerates the evolution of antifungal drug resistance in Candida albicans

Project description:Mistranslation accelerates the evolution of antifungal drug resistance in Candida albicans

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Mistranslation accelerates the evolution of antifungal drug resistance in Candida albicans [CGH]

Project description:The fungal pathogen Candida albicans and other pathogens of the CTG clade reassigned the leucine CUG codon to serine and tolerate highly variable levels of both serine and leucine at CUG positions in response to environmental cues. Previous studies found that increased leucine misincorporation levels enhance resistance to drugs but the underlying mechanisms are not known. To clarify the biological role of this tuneable codon ambiguity, we evolved C. albicans strains engineered to mistranslate CUG at elevated levels, in the presence and absence of the antifungal drug fluconazole

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Mistranslation accelerates the evolution of antifungal drug resistance in Candida albicans [Gene expression]

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Mistranslation accelerates the adaptation of Candida albicans to Fluconazole

Project description:The leucine CUG codon was reassigned to serine in the fungal pathogen Candida albicans. To clarify the biological role of this tuneable codon ambiguity on drug resistance, we evolved C. albicans strains that were engineered to mistranslate the CUG codon at constitutively elevated levels, in the presence and absence of the antifungal drug fluconazole. Elevated levels of mistranslation resulted in the rapid acquisition of resistance to fluconazole.

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Project description:Mistranslation accelerates the evolution of antifungal drug resistance in Candida albicans [CGH]

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Antifungal Activity of Mammalian Serum amyloid A1 against Candida albicans

Project description:Human serum amyloid A (SAA) is a major acute phase protein and shows a massive increase of concentration in plasma during inflammation. In the current study, we report that recombinant human and mouse SAA1 (rhSAA1 and rmSAA1) have a potent antifungal activity against the major fungal pathogen Candida albicans. rhSAA1 binds to the cell surface of C. albicans and promotes cell aggregation. At high concentrations, rhSAA1 disrupts the membrane integrity and induces rapid cell death of C. albicans. Further investigation demonstrates that rhSAA1 targets on the cell wall adhesin Als3 of C. albicans. Inactivation of ALS3 in C. albicans leads to remarkably decreased cell aggregation and death upon rhSAA1 treatment, implying that Als3 plays a critical role in SAA1 sensing. Moreover, deletion of the ALS3 transcriptional regulators such as AHR1, BCR1, and EFG1 in C. albicans results in a similar effect on cell responses to that of the als3/als3 mutant upon rhSAA1 treatment. Global gene expression profiling analysis indicates that rhSAA1 has a remarkable impact on the expression of cell wall- and metabolism-related genes in C. albicans. Our finding of the antifungal activity of rhSAA1 against C. albicans expands the function of this protein and would provide new insights into the understanding of the host-Candida interaction during infections.

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Mistranslation accelerates the evolution of antifungal drug resistance in Candida albicans

Project description:This SuperSeries is composed of the SubSeries listed below.

2017-07-18 | GSE60122 | GEO

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Project description:Mistranslation accelerates the evolution of antifungal drug resistance in Candida albicans [Gene expression]

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Analysis of protein biosynthesis errors in Candida albicans.

Project description:Recent works show that protein mistranslation is widespread in nature and that both single cell or multicellular organisms can take advantage of it, by regulating its levels, under specific physiological and environmental conditions. In C. albicans, it leads to increased morphological and physiological phenotypic diversity of high adaptive potential, but the scope of such protein mistranslation is poorly understood due to technical difficulties in detecting and quantifying amino acid misincorporation events in complex proteomic samples. The phenomenon of mistranslation has been extensively studied in the leucine CUG codon, which has been reassigned to either serine or alanine, or ambiguously assigned to serine and leucine in several fungal species of the so called CTG clade. Serine-to-leucine (Ser→Leu) ambiguous decoding has been observed in Ascoidea asiatica, Candida maltosa, C. albicans and more recently, in the halotolerant yeast Debaryomyces hansenii. In C. albicans, CUG translation is facilitated by a hybrid tRNA(CAG)Ser that contains identity elements for both seryl-tRNA synthetase (SerRS) and leucyl-tRNA synthetase (LeuRS). Under normal physiological conditions the tRNA(CAG)Ser is mainly aminoacylated with Ser by the SerRS (appx 97%). We have developed and optimized mass spectrometry and bioinformatics pipelines capable of identifying low-level amino acid misincorporation events at the proteome level and determine codons error frequencies. We have also analysed the proteomic profile of an engineered C. albicans strain that exhibits high level of leucine misincorporation at protein CUG sites.

2024-09-09 | PXD047025 | Pride

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