Amino acid substitution in <i>Cryptococcus neoformans</i> lanosterol 14-α-demethylase involved in fluconazole resistance in clinical isolates
The molecular basis of fluconazole resistance in <i>Cryptococcus neoformans</i> has been poorly studied. A common azole resistance mechanism in <i>Candida</i> species is the acquisition of point mutations in the <i>ERG11</i> gene encoding the enzyme lanosterol 14-...
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| Autores principales: | , , , , , , |
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| Formato: | Articulo |
| Lenguaje: | Inglés |
| Publicado: |
2016
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| Materias: | |
| Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/106345 https://www.sciencedirect.com/science/article/pii/S0325754116300013 |
| Aporte de: |
| Sumario: | The molecular basis of fluconazole resistance in <i>Cryptococcus neoformans</i> has been poorly studied. A common azole resistance mechanism in <i>Candida</i> species is the acquisition of point mutations in the <i>ERG11</i> gene encoding the enzyme lanosterol 14-α-demethylase, target of the azole class of drugs. In <i>C. neoformans</i> only two mutations were described in this gene. In order to evaluate other mutations that could be implicated in fluconazole resistance in <i>C. neoformans</i> we studied the genomic sequence of the <i>ERG11</i> gene in 11 clinical isolates with minimal inhibitory concentration (MIC) values to fluconazole of ≥16 μg/ml. The sequencing revealed the G1855A mutation in 3 isolates, resulting in the enzyme amino acid substitution G484S. These strains were isolated from two fluconazole-treated patients. This mutation would not intervene in the susceptibility to itraconazole and voriconazole. |
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