A Phe389Leu substitution in ergA confers terbinafine resistance in Aspergillus fumigatus.
Replacement of phenylalanine with leucine at position 391 in squalene epoxidase was identified as being responsible for terbinafine resistance in mutants of Aspergillus nidulans. The equivalent mutation was engineered into the ergA gene of Aspergillus fumigatus, resulting in an F389L substitution that also conferred resistance to this pathogenic mold.
Rocha
E M F
EM
Public Health Research Institute, International Center for Public Health, Newark, NJ 07103-3535, USA.
Gardiner
R E
RE
Park
S
S
Martinez-Rossi
N M
NM
Perlin
D S
DS
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000935:Antifungal Agents / Q000494:pharmacology*; D001232:Aspergillus fumigatus / Q000187:drug effects* / Q000201:enzymology / Q000235:genetics; D025141:Drug Resistance, Fungal / Q000235:genetics*; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D009281:Naphthalenes / Q000494:pharmacology*; D050603:Squalene Monooxygenase / Q000737:chemistry / Q000235:genetics*; D000077291:Terbinafine
D000935:Antifungal Agents; D005656:Fungal Proteins; D009281:Naphthalenes; D050603:Squalene Monooxygenase; D000077291:Terbinafine