A Phe389Leu substitution in ergA confers terbinafine resistance in Aspergillus fumigatus

Antimicrob Agents Chemother. 2006 Jul;50(7):2533-6. doi: 10.1128/AAC.00187-06.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution*
  • Antifungal Agents / pharmacology*
  • Aspergillus fumigatus / drug effects*
  • Aspergillus fumigatus / enzymology
  • Aspergillus fumigatus / genetics
  • Drug Resistance, Fungal / genetics*
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Naphthalenes / pharmacology*
  • Squalene Monooxygenase / chemistry
  • Squalene Monooxygenase / genetics*
  • Terbinafine

Substances

  • Antifungal Agents
  • Fungal Proteins
  • Naphthalenes
  • Squalene Monooxygenase
  • Terbinafine