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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

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.

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* 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.

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

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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.

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