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Applied and Environmental Microbiology, March 2006, p. 1739-1748, Vol. 72, No. 3
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.3.1739-1748.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Sedolisins, a New Class of Secreted Proteases from Aspergillus fumigatus with Endoprotease or Tripeptidyl-Peptidase Activity at Acidic pHs{dagger}

Utz Reichard,1* Barbara Léchenne,2 Abdul R. Asif,3 Frank Streit,3 Eric Grouzmann,4 Olivier Jousson,5 and Michel Monod2

Department of Medical Microbiology and National Reference Center for Systemic Mycoses,1 Department of Clinical Chemistry, University Hospital of Göttingen, Göttingen, Germany,3 Service de Dermatologie et Vénéréologie,2 Division de Pharmacologie et Toxicologie Cliniques, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland,4 Dipartimento di Patologia Animale, Profilassi e Igiene degli Alimenti, Università di Pisa, Pisa, Italy5

Received 18 May 2005/ Accepted 5 November 2005

The secreted proteolytic activity of Aspergillus fumigatus is of potential importance as a virulence factor and in the industrial hydrolysis of protein sources. The A. fumigatus genome contains sequences that could encode a five-member gene family that produces proteases in the sedolisin family (MEROPS S53). Four putative secreted sedolisins with a predicted 17- to 20-amino-acid signal sequence were identified and termed SedA to SedD. SedA produced heterologously in Pichia pastoris was an acidic endoprotease. Heterologously produced SedB, SedC, and SedD were tripeptidyl-peptidases (TPP) with a common specificity for tripeptide-p-nitroanilide substrates at acidic pHs. Purified SedB hydrolyzed the peptide Ala-Pro-Gly-Asp-Arg-Ile-Tyr-Val-His-Pro-Phe to Arg-Pro-Gly, Asp-Arg-Ile, and Tyr-Val-His-Pro-Phe, thereby confirming TPP activity of the enzyme. SedB, SedC, and SedD were detected by Western blotting in culture supernatants of A. fumigatus grown in a medium containing hemoglobin as the sole nitrogen source. A degradation product of SedA also was observed. A search for genes encoding sedolisin homologues in other fungal genomes indicates that sedolisin gene families are widespread among filamentous ascomycetes.

* Corresponding author. Mailing address: Department of Medical Microbiology, University Hospital of Göttingen, Kreuzbergring 57, D-37075 Göttingen, Germany. Phone: 49-551-395-856. Fax: 49-551-395-860. E-mail: ureicha{at}gwdg.de.

{dagger} Supplementary material for this article may be found at http://aem.asm.org/.

Applied and Environmental Microbiology, March 2006, p. 1739-1748, Vol. 72, No. 3
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.3.1739-1748.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hohl, T. M., Feldmesser, M. (2007). Aspergillus fumigatus: Principles of Pathogenesis and Host Defense. Eukaryot Cell 6: 1953-1963 [Full Text]  


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