Sulphite efflux pumps in Aspergillus fumigatus and dermatophytes.

Détails

ID Serval
serval:BIB_5BF31B2093F0
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Sulphite efflux pumps in Aspergillus fumigatus and dermatophytes.
Périodique
Microbiology
Auteur(s)
Léchenne B., Reichard U., Zaugg C., Fratti M., Kunert J., Boulat O., Monod M.
ISSN
1350-0872
Statut éditorial
Publié
Date de publication
03/2007
Peer-reviewed
Oui
Volume
153
Numéro
Pt 3
Pages
905-913
Langue
anglais
Notes
Publication types: Journal Article. - Old month value: Mar
Résumé
Dermatophytes and other filamentous fungi excrete sulphite as a reducing agent during keratin degradation. In the presence of sulphite, cystine in keratin is directly cleaved to cysteine and S-sulphocysteine, and thereby, reduced proteins become accessible to hydrolysis by a variety of secreted endo- and exoproteases. A gene encoding a sulphite transporter in Aspergillus fumigatus (AfuSSU1), and orthologues in the dermatophytes Trichophyton rubrum and Arthroderma benhamiae (TruSSU1 and AbeSSU1, respectively), were identified by functional expression in Saccharomyces cerevisiae. Like the S. cerevisiae sulphite efflux pump Ssu1p, AfuSsu1p, TruSsu1p and AbeSsu1p belong to the tellurite-resistance/dicarboxylate transporter (TDT) family which includes the Escherichia coli tellurite transporter TehAp and the Schizosaccharomyces pombe malate transporter Mae1p. Seven genes in the A. fumigatus genome encode transporters of the TDT family. However, gene disruption of AfuSSU1 and of the two more closely related paralogues revealed that only AfuSSU1 encodes a sulphite efflux pump. TruSsulp and AbeSsulp are believed to be the first members of the TDT family identified in dermatophytes. The relatively high expression of TruSSU1 and AbeSSU1 in dermatophytes compared to that of AfuSSU1 in A. fumigatus likely reflects a property of dermatophytes which renders these fungi pathogenic. Sulphite transporters could be a new target for antifungal drugs in dermatology, since proteolytic digestion of hard keratin would not be possible without prior reduction of disulphide bridges.
Mots-clé
ATP-Binding Cassette Transporters/physiology, Antifungal Agents/metabolism, Antifungal Agents/pharmacology, Arthrodermataceae/genetics, Arthrodermataceae/metabolism, Aspergillus fumigatus/genetics, Aspergillus fumigatus/metabolism, Base Sequence, Cloning, Molecular, DNA, Fungal/chemistry, DNA, Fungal/genetics, Drug Resistance, Fungal, Escherichia coli/genetics, Gene Expression, Molecular Sequence Data, Phylogeny, Saccharomyces cerevisiae/drug effects, Saccharomyces cerevisiae/genetics, Schizosaccharomyces/genetics, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Sulfites/metabolism, Sulfites/pharmacology, Trichophyton/genetics, Trichophyton/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/01/2008 16:46
Dernière modification de la notice
20/08/2019 14:14
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