Research from University of Liege, Center for Protein Engineering in the area of allergies described
December 22nd, 2008
2008 DEC 22 -- Data detailed in 'Activation mechanism of recombinant Der p 3 allergen zymogen: contribution of cysteine protease Der p 1 and effect of propeptide glycosylation' have been presented. "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," scientists in Liege, Belgium report.
"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," wrote M.E. Dumez and colleagues, University of Liege, Center for Protein Engineering.
The researchers concluded: "Finally, we showed that recombinant Der p 3 is inhibited by the free modified prosequence T(P1)R."
Dumez and colleagues published their study in the Journal of Biological Chemistry (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).
For additional information, contact M.E. Dumez, Universite de Liege, Centre for Protein Engineering, Centre de Recherches du Cyclotron, Liege 4000, Belgium.
The publisher's contact information for the Journal of Biological Chemistry is: American Society Biochemistry Molecular Biology Inc., 9650 Rockville Pike, Bethesda, MD 20814-3996, USA.
