Please use this identifier to cite or link to this item:http://hdl.handle.net/20.500.12105/8247
G484S amino acid substitution in lanosterol 14-alpha demethylase (ERG11) is related to fluconazole resistance in a recurrent Cryptococcus neoformans clinical isolate
Antimicrob Agents Chemother. 2003 Nov;47(11):3653-6.
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.
Acquired Immunodeficiency Syndrome | Adult | Amino Acid Sequence | Amino Acid Substitution | Antifungal Agents | Cloning, Molecular | Cryptococcus neoformans | Cytochrome P-450 Enzyme System | Drug Resistance, Fungal | Fluconazole | Genotype | Humans | Male | Meningitis, Cryptococcal | Microbial Sensitivity Tests | Molecular Sequence Data | Oxidoreductases | Plasmids | Point Mutation | Recurrence | Sterol 14-Demethylase