Arnd Petersen
Dr. Arnd Petersen
Research Center Borstel
Biochemical and Molecular Allergology
Parkallee 22
D-23845 Borstel, Germany
Phone: +49 (4537) 188 497
Fax: +49 (4537) 188 404
eMail: apeters@fz-borstel.de
A. PETERSEN (a), K. GROBE (a), G. SCHRAMM (a), K. GEHLHAR (a), S. VIETHS (b), F. ALTMANN (c), M. SCHLAAK (a), W.-M. BECKER (a)
(a) Research Center Borstel, Biochemical and Molecular Allergology,
Borstel, Germany
(b) Paul-Ehrlich-Institute, Department of Allergology, Langen, Germany
(c) Institute of Chemistry, University of Agriculture, Vienna, Austria
| SUMMARY |
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| The structure of an allergen plays a crucial role in
type I allergy. It is involved in the sensitization process as well as
in allergic reactions that are caused by repetitive exposure. Here, we
focused on the abundant group I allergens of grass pollen, which are known
for their IgE inducing potential. We identified at least four independent
IgE-binding regions (conformational epitopes) on the molecule. A few continuous
epitopes were determined, but they seem to be of minor relevance. As regards
post-translational modifications we detected disulfide formations, one
N-glycan of the complex type and two hydroxylated proline residues. All
these modifications increased the allergenicity. Additionally it was shown
that IgE cross-reactivity to unrelated proteins such as tomato is caused
by similarities in carbohydrate moieties.
Like several food allergens e.g. Act c 1 (kiwi fruit), Gly mBd 30K (soybean) and the dust mite allergen Der p 1, the grass pollen allergen Phl p 1 is a cysteine protease. We proved this by use of specific substrates, specific inhibitors, and by comparison of the protein sequences. In analogy to Der p 1 we deduce that Phl p 1 might enhance the permeability of the epithelium, influence T helper cells to cause a bias to Th2, and increase the IgE production of plasma cells. Thus, the group I allergens seem to be important components in a pollen extract which can mediate sensitization and enhance the triggering of symptoms leading to a persistence of grass pollen allergy. |
type I allergy post-translational modifications epitope mapping protease
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[Introduction] [IgE-reactive Epitopes] [Protein Function] [Implications] [References] [Abbreveations]
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Arnd Petersen |
Correspondence:
Dr. Arnd Petersen Research Center Borstel Biochemical and Molecular Allergology Parkallee 22 D-23845 Borstel, Germany Phone: +49 (4537) 188 497
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home: www.food-allergens.de |