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Article

G484S amino acid substitution in lanosterol 14-alpha demethylase (ERG11) is related to fluconazole resistance in a recurrent Cryptococcus neoformans clinical isolate.

Antimicrobial agents and chemotherapy - 1 Nov 2003

Rodero Laura, Mellado Emilia, Rodriguez A Carolina, Salve Angela, Guelfand Liliana, Cahn Pedro, Cuenca-Estrella Manuel, Davel Graciela, Rodriguez-Tudela Juan L

Abstract excerpt

Five sequential Cryptococcus neoformans isolates recovered from an AIDS patient with recurrent meningitis were analyzed. Four isolates were fluconazole susceptible, while the fifth isolate developed fluconazole resistance. Analysis of the 14-alpha lanosterol demethylase gene (ERG11) showed a point mutation in the resistant strain responsible for the amino acid substitution G484S.

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 14576140
DOI: 10.1128/AAC.47.11.3653-3656.2003
PMCID: PMC253790

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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G484S amino acid substitution in lanosterol 14-alpha demethylase (ERG11) is related to fluconazole resistance in a recurrent Cryptococcus neoformans clinical isolate.PMID 14576140Read ↗

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Cloning and characterization of the lanosterol 14alpha-demethylase (ERG11) gene in Cryptococcus neoformans.Semantic proximity Read ↗

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