Isolation and characterization of a secreted metalloprotease of Aspergillus fumigatus.

Détails

ID Serval
serval:BIB_9DC8CA5E7817
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Isolation and characterization of a secreted metalloprotease of Aspergillus fumigatus.
Périodique
Infection and Immunity
Auteur(s)
Monod M., Paris S., Sanglard D., Jaton-Ogay K., Bille J., Latgé J.P.
ISSN
0019-9567 (Print)
ISSN-L
0019-9567
Statut éditorial
Publié
Date de publication
1993
Volume
61
Numéro
10
Pages
4099-4104
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
A metalloprotease (MEP) secreted by Aspergillus fumigatus was isolated from an alkaline protease-deficient mutant after the fungus was cultivated in the presence of collagen as the sole nitrogen and carbon source. The enzyme was purified 50-fold from the culture supernatant after adsorption to hydroxylapatite and carboxy-methyl-Sephadex and after gel filtration. The molecular mass was determined to be 40 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point was estimated at pH 5.5 by isoelectric focusing. Reducing agents and divalent cations strongly inhibited enzyme activity, whereas nonionic detergents had no effect. A. fumigatus MEP was totally inhibited by EDTA, 1,10-phenanthroline, and phosphoramidon but not by inhibitors specific for serine, aspartate, and cysteine proteases. MEP is not able to cleave elastin and is thermosensitive. Sera from patients suffering from aspergilloma reacted with MEP in Western blotting (immunoblotting) analyses, suggesting that MEP promotes an antigenic response in these patients.
Mots-clé
Antibodies, Fungal/immunology, Antigens, Fungal/chemistry, Antigens, Fungal/immunology, Aspergillosis/immunology, Aspergillus fumigatus/enzymology, Cations, Divalent, Detergents, Glycoproteins/chemistry, Humans, Metalloendopeptidases/antagonists &amp, inhibitors, Metalloendopeptidases/chemistry, Molecular Weight, Oxidation-Reduction, Protease Inhibitors/pharmacology, Solvents, Temperature
Pubmed
Web of science
Création de la notice
25/01/2008 16:46
Dernière modification de la notice
20/08/2019 15:04
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