A Ser678Pro substitution in Fks1p confers resistance to echinocandin drugs in Aspergillus fumigatus

Antimicrob Agents Chemother. 2007 Nov;51(11):4174-6. doi: 10.1128/AAC.00917-07. Epub 2007 Aug 27.

Abstract

An S678P substitution in Fks1p, the major subunit of glucan synthase, was sufficient to confer echinocandin resistance in Aspergillus fumigatus. The equivalent mutation in Candida spp. has been implicated in echinocandin resistance. This work demonstrates that modification of Fks1p is a conserved mechanism for echinocandin resistance in pathogenic fungi.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution*
  • Aspergillus fumigatus / drug effects*
  • Aspergillus fumigatus / genetics
  • Drug Resistance, Fungal / genetics*
  • Echinocandins / pharmacology*
  • Fungal Proteins / antagonists & inhibitors
  • Fungal Proteins / genetics
  • Glucosyltransferases / antagonists & inhibitors
  • Glucosyltransferases / genetics*
  • Molecular Sequence Data
  • Proline / genetics
  • Sequence Homology, Amino Acid
  • Serine / genetics

Substances

  • Echinocandins
  • Fungal Proteins
  • Serine
  • Proline
  • Glucosyltransferases
  • glucan synthase