A Phe389Leu Substitution in ErgA Confers Terbinafine Resistance in Aspergillus fumigatus
Author(s) -
Eleusa Maria Ferreira Rocha,
R. E. Gardiner,
S. Park,
Nilce Maria Martinez-Rossi,
David S. Perlin
Publication year - 2006
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.00187-06
Subject(s) - aspergillus fumigatus , aspergillus nidulans , aspergillus , microbiology and biotechnology , terbinafine , biology , mutant , squalene monooxygenase , gene , genetics , biosynthesis , antifungal , itraconazole
Replacement of phenylalanine with leucine at position 391 in squalene epoxidase was identified as being responsible for terbinafine resistance in mutants ofAspergillus nidulans . The equivalent mutation was engineered into theergA gene ofAspergillus fumigatus , resulting in an F389L substitution that also conferred resistance to this pathogenic mold.
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