Biochemical and antigenic characterization of a new dipeptidyl-peptidase isolated from Aspergillus fumigatus

被引:96
作者
Beauvais, A
Monod, M
Debeaupuis, JP
Diaquin, M
Kobayashi, H
Latge, JP
机构
[1] CHU VAUDOIS, DERMATOL SERV, LAUSANNE, SWITZERLAND
[2] TOHOKU COLL PHARMACEUT SCI, DEPT HYG CHEM, AOBA KU, SENDAI, MIYAGI, JAPAN
关键词
D O I
10.1074/jbc.272.10.6238
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A novel dipeptidyl-peptidase (DPP V) was purified from the culture medium of Aspergillus fumgatus. 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, Ris-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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页码:6238 / 6244
页数:7
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