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: Bosco Borgeat, María E., Mazza, Mariana, Taverna, Constanza G., Córdoba, Susana Beatriz, Murisengo, Omar A., Vivot, Walter, Davel, Graciela
Formato: Articulo
Lenguaje:Inglés
Publicado: 2016
Materias:
Ciencias Veterinarias
Ciencias Médicas
Cryptococcus neoformans
Fluconazole resistance
ERG11 gene
amino acid substitution
mutation
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/106345
https://www.sciencedirect.com/science/article/pii/S0325754116300013
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-106345
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Veterinarias
Ciencias Médicas
Cryptococcus neoformans
Fluconazole resistance
ERG11 gene
amino acid substitution
mutation
spellingShingle Ciencias Veterinarias
Ciencias Médicas
Cryptococcus neoformans
Fluconazole resistance
ERG11 gene
amino acid substitution
mutation
Bosco Borgeat, María E.
Mazza, Mariana
Taverna, Constanza G.
Córdoba, Susana Beatriz
Murisengo, Omar A.
Vivot, Walter
Davel, Graciela
Amino acid substitution in <i>Cryptococcus neoformans</i> lanosterol 14-α-demethylase involved in fluconazole resistance in clinical isolates
topic_facet Ciencias Veterinarias
Ciencias Médicas
Cryptococcus neoformans
Fluconazole resistance
ERG11 gene
amino acid substitution
mutation
description 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.
format Articulo
Articulo
author Bosco Borgeat, María E.
Mazza, Mariana
Taverna, Constanza G.
Córdoba, Susana Beatriz
Murisengo, Omar A.
Vivot, Walter
Davel, Graciela
author_facet Bosco Borgeat, María E.
Mazza, Mariana
Taverna, Constanza G.
Córdoba, Susana Beatriz
Murisengo, Omar A.
Vivot, Walter
Davel, Graciela
author_sort Bosco Borgeat, María E.
title Amino acid substitution in <i>Cryptococcus neoformans</i> lanosterol 14-α-demethylase involved in fluconazole resistance in clinical isolates
title_short Amino acid substitution in <i>Cryptococcus neoformans</i> lanosterol 14-α-demethylase involved in fluconazole resistance in clinical isolates
title_full Amino acid substitution in <i>Cryptococcus neoformans</i> lanosterol 14-α-demethylase involved in fluconazole resistance in clinical isolates
title_fullStr Amino acid substitution in <i>Cryptococcus neoformans</i> lanosterol 14-α-demethylase involved in fluconazole resistance in clinical isolates
title_full_unstemmed Amino acid substitution in <i>Cryptococcus neoformans</i> lanosterol 14-α-demethylase involved in fluconazole resistance in clinical isolates
title_sort amino acid substitution in <i>cryptococcus neoformans</i> lanosterol 14-α-demethylase involved in fluconazole resistance in clinical isolates
publishDate 2016
url http://sedici.unlp.edu.ar/handle/10915/106345
https://www.sciencedirect.com/science/article/pii/S0325754116300013
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