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Activation mechanism of recombinant Der p 3 allergen zymogen: contribution of cysteine protease Der p 1 and effect of propeptide glycosylation

Marie-Eve Dumez, Nathalie Teller, Frédéric Mercier, Tetsuya Tanaka, Isabel Vandenberghe UGent, Michel Vandenbranden, Bart Devreese UGent, André Luxen, Jean-Marie Frère and André Matagne, et al. (2008) JOURNAL OF BIOLOGICAL CHEMISTRY. 283(45). p.30606-30617
abstract
The trypsin-like protease Der p 3, a major allergen of the house dust mite Dermatophagoides pteronyssinus, is synthesized as a zymogen, termed proDer p 3. No recombinant source of Der p 3 has been described yet, and the zymogen maturation mechanism remains to be elucidated. The Der p 3 zymogen was produced in Pichia pastoris. We demonstrated that the recombinant zymogen is glycosylated at the level of its propeptide. We showed that the activation mechanism of proDer p 3 is intermolecular and is mediated by the house dust mite cysteine protease Der p 1. The primary structure of the proDer p 3 propeptide is associated with a unique zymogen activation mechanism, which is different from those described for the trypsin-like family and relies on the house dust mite papain-like protease Der p 1. This is the first report of a recombinant source of Der p 3, with the same enzymatic activity as the natural enzyme and trypsin. Glycosylation of the propeptide was found to decrease the rate of maturation. Finally, we showed that recombinant Der p 3 is inhibited by the free modified prosequence T(P1)R.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
J. Biol. Chem.
volume
283
issue
45
pages
30606 - 30617
Web of Science type
Article
Web of Science id
000260544800084
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
5.52 (2008)
JCR rank
47/276 (2008)
JCR quartile
1 (2008)
ISSN
0021-9258
DOI
10.1074/jbc.M803041200
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
594767
handle
http://hdl.handle.net/1854/LU-594767
date created
2009-04-16 13:49:22
date last changed
2012-10-23 14:58:41
@article{594767,
  abstract     = {The trypsin-like protease Der p 3, a major allergen of the house dust mite Dermatophagoides pteronyssinus, is synthesized as a zymogen, termed proDer p 3. No recombinant source of Der p 3 has been described yet, and the zymogen maturation mechanism remains to be elucidated. The Der p 3 zymogen was produced in Pichia pastoris. We demonstrated that the recombinant zymogen is glycosylated at the level of its propeptide. We showed that the activation mechanism of proDer p 3 is intermolecular and is mediated by the house dust mite cysteine protease Der p 1. The primary structure of the proDer p 3 propeptide is associated with a unique zymogen activation mechanism, which is different from those described for the trypsin-like family and relies on the house dust mite papain-like protease Der p 1. This is the first report of a recombinant source of Der p 3, with the same enzymatic activity as the natural enzyme and trypsin. Glycosylation of the propeptide was found to decrease the rate of maturation. Finally, we showed that recombinant Der p 3 is inhibited by the free modified prosequence T(P1)R.},
  author       = {Dumez, Marie-Eve and Teller, Nathalie and Mercier, Fr{\'e}d{\'e}ric and Tanaka, Tetsuya and Vandenberghe, Isabel and Vandenbranden, Michel and Devreese, Bart and Luxen, Andr{\'e} and Fr{\`e}re, Jean-Marie and Matagne, Andr{\'e} and Jacquet, Alain and Galleni, Moreno and Chevign{\'e}, Andy},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  language     = {eng},
  number       = {45},
  pages        = {30606--30617},
  title        = {Activation mechanism of recombinant Der p 3 allergen zymogen: contribution of cysteine protease Der p 1 and effect of propeptide glycosylation},
  url          = {http://dx.doi.org/10.1074/jbc.M803041200},
  volume       = {283},
  year         = {2008},
}

Chicago
Dumez, Marie-Eve, Nathalie Teller, Frédéric Mercier, Tetsuya Tanaka, Isabel Vandenberghe, Michel Vandenbranden, Bart Devreese, et al. 2008. “Activation Mechanism of Recombinant Der p 3 Allergen Zymogen: Contribution of Cysteine Protease Der p 1 and Effect of Propeptide Glycosylation.” Journal of Biological Chemistry 283 (45): 30606–30617.
APA
Dumez, M.-E., Teller, N., Mercier, F., Tanaka, T., Vandenberghe, I., Vandenbranden, M., Devreese, B., et al. (2008). Activation mechanism of recombinant Der p 3 allergen zymogen: contribution of cysteine protease Der p 1 and effect of propeptide glycosylation. JOURNAL OF BIOLOGICAL CHEMISTRY, 283(45), 30606–30617.
Vancouver
1.
Dumez M-E, Teller N, Mercier F, Tanaka T, Vandenberghe I, Vandenbranden M, et al. Activation mechanism of recombinant Der p 3 allergen zymogen: contribution of cysteine protease Der p 1 and effect of propeptide glycosylation. JOURNAL OF BIOLOGICAL CHEMISTRY. 2008;283(45):30606–17.
MLA
Dumez, Marie-Eve, Nathalie Teller, Frédéric Mercier, et al. “Activation Mechanism of Recombinant Der p 3 Allergen Zymogen: Contribution of Cysteine Protease Der p 1 and Effect of Propeptide Glycosylation.” JOURNAL OF BIOLOGICAL CHEMISTRY 283.45 (2008): 30606–30617. Print.