Luxen, André[Université de Liège - ULg > Département de chimie (sciences) > Chimie organique de synthèse - Centre de recherches du cyclotron >]
Frère, Jean-Marie[Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Matagne, André[Université de Liège - ULg > Département des sciences de la vie > Enzymologie et repliement des protéines, Centre d'Ingénierie des Protéines > >]
American Society for Biochemistry and Molecular Biology
283
45
30606-30617
International
0021-9258
1083-351X
Baltimore
MD
[en] 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 TP1R.
[Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques, Centre d'Ingénierie des Protéines > >]
