Mellado, EmiliaGarcia-Effron, GuillermoAlcazar-Fuoli, LauraCuenca-Estrella, ManuelRodriguez-Tudela, Juan Luis2019-08-142019-08-142004-07Antimicrob Agents Chemother. 2004 Jul;48(7):2747-50.0066-4804http://hdl.handle.net/20.500.12105/8260Five clinical isolates of Aspergillus fumigatus that exhibited similar patterns of reduced susceptibility to itraconazole and other triazole drugs were analyzed. Sequence analysis of genes (cyp51A and cyp51B) encoding the 14alpha-sterol demethylases revealed that all five strains harbored mutations in cyp51A resulting in the replacement of methionine at residue 220 by valine, lysine, or threonine. When the mutated cyp51A genes were introduced into an A. fumigatus wild-type strain, the transformants exhibited reduced susceptibility to all triazole agents, confirming that the mutations were responsible for the resistance phenotype.engAMhttp://creativecommons.org/licenses/by-nc-sa/4.0/AllelesAmino Acid SequenceAmino Acid SubstitutionAntifungal AgentsAspergillus fumigatusAzolesCytochrome P-450 Enzyme SystemDrug Resistance, FungalFungal ProteinsMethionineMicrobial Sensitivity TestsMolecular Sequence DataMutationReverse Transcriptase Polymerase Chain ReactionSubstitutions at methionine 220 in the 14alpha-sterol demethylase (Cyp51A) of Aspergillus fumigatus are responsible for resistance in vitro to azole antifungal drugsAtribución-NoComercial-CompartirIgual 4.0 Internacional152151424872747-5010.1128/AAC.48.7.2747-2750.2004Antimicrobial agents and chemotherapyopen access