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Volume 272, Number 10, Issue of March 7, 1997 pp. 6238-6244
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Biochemical and Antigenic Characterization of a New Dipeptidyl-Peptidase Isolated from Aspergillus fumigatus

(Received for publication, September 22, 1996, and in revised form, December 24, 1996)

Anne Beauvais , Michel Monod ^¶ , Jean-Paul Debeaupuis , Michel Diaquin , Hidemitsu Kobayashi and Jean-Paul Latgé

From the  Laboratoire des Aspergillus, Institut Pasteur, Paris, France, ^¶ Service de Dermatologie, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland, and the  Department of Hygienic Chemistry, Tohoku College of Pharmacy, Aoba-ku, Sendai, Japan

A novel dipeptidyl-peptidase (DPP V) was purified from the culture medium of Aspergillus fumigatus. This is the first report of a secreted dipeptidyl-peptidase. The enzyme had a molecular mass of 88 kDa and contained approximately 9 kDa of N-linked carbohydrate. The expression and secretion of dipeptidyl-peptidase varied with the growth conditions; maximal intra- and extracellular levels were detected when the culture medium contained only proteins or protein hydrolysates in the absence of sugars. The gene of DPP V was cloned and showed significant sequence homology to other eukaryotic dipeptidyl-peptidase genes. Unlike the other dipeptidyl-peptidases, which are all intracellular, DPP V contained a signal peptide. Like the genes of other dipeptidyl-peptidases, that of DPP V displayed the consensus sequences of the catalytic site of the nonclassical serine proteases. The biochemical properties of native and recombinant DPP V obtained in Pichia pastoris were unique and were characterized by a substrate specificity limited to the hydrolysis of X-Ala, His-Ser, and Ser-Tyr dipeptides at a neutral pH optimum. In addition, we showed that DPP V is identical to one of the two major antigens used for the diagnosis of aspergillosis.

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