SCOPE: Celery represents a relevant cross-reactive food allergen source in the adult population. As the currently known allergens are not typical elicitors of severe symptoms, we aimed to identify and characterize a non-specific lipid transfer protein (nsLTP). METHODS AND RESULTS: MS and cDNA cloning were applied to obtain the full-length sequence of a novel allergenic nsLTP from celery stalks. The purified natural molecule consisted of a single isoallergen designated as Api g 2.0101, which was recombinantly produced in Escherichia coli Rosetta-gami. The natural and recombinant molecules displayed equivalent physicochemical and immunological properties. Circular dichroism revealed a typical α-helical fold and high thermal stability. Moreover, Api g 2 was highly resistant to simulated gastrointestinal digestion. As assessed by ELISA, thermal denaturation did not affect the IgE binding of Api g 2. Natural and recombinant Api g 2 showed similar allergenic activity in mediator release assays. Api g 2-specific IgE antibodies cross-reacted with peach and mugwort pollen nsLTPs. CONCLUSION: Based on our results, it can be anticipated that inclusion of recombinant Api g 2 in the current panel of allergens for molecule-based diagnosis will facilitate the evaluation of the clinical relevance of nsLTP sensitization in celery allergy and help clinicians in the management of food allergic patients.
SCOPE: Celery represents a relevant cross-reactive food allergen source in the adult population. As the currently known allergens are not typical elicitors of severe symptoms, we aimed to identify and characterize a non-specific lipid transfer protein (nsLTP). METHODS AND RESULTS: MS and cDNA cloning were applied to obtain the full-length sequence of a novel allergenic nsLTP from celery stalks. The purified natural molecule consisted of a single isoallergen designated as Api g 2.0101, which was recombinantly produced in Escherichia coli Rosetta-gami. The natural and recombinant molecules displayed equivalent physicochemical and immunological properties. Circular dichroism revealed a typical α-helical fold and high thermal stability. Moreover, Api g 2 was highly resistant to simulated gastrointestinal digestion. As assessed by ELISA, thermal denaturation did not affect the IgE binding of Api g 2. Natural and recombinant Api g 2 showed similar allergenic activity in mediator release assays. Api g 2-specific IgE antibodies cross-reacted with peach and mugwort pollen nsLTPs. CONCLUSION: Based on our results, it can be anticipated that inclusion of recombinant Api g 2 in the current panel of allergens for molecule-based diagnosis will facilitate the evaluation of the clinical relevance of nsLTP sensitization in celeryallergy and help clinicians in the management of food allergicpatients.
Authors: Martina Di Muzio; Sabrina Wildner; Sara Huber; Michael Hauser; Eva Vejvar; Werner Auzinger; Christof Regl; Josef Laimer; Danila Zennaro; Nicole Wopfer; Christian G Huber; Ronald van Ree; Adriano Mari; Peter Lackner; Fatima Ferreira; Mario Schubert; Gabriele Gadermaier Journal: J Biol Chem Date: 2020-12-18 Impact factor: 5.157
Authors: Martina Di Muzio; Sabrina Wildner; Sara Huber; Michael Hauser; Eva Vejvar; Werner Auzinger; Christof Regl; Josef Laimer; Danila Zennaro; Nicole Wopfner; Christian G Huber; Ronald van Ree; Adriano Mari; Peter Lackner; Fatima Ferreira; Mario Schubert; Gabriele Gadermaier Journal: J Biol Chem Date: 2020-10-09 Impact factor: 5.157
Authors: Stephanie Eichhorn; Angelika Hörschläger; Markus Steiner; Josef Laimer; Bettina M Jensen; Serge A Versteeg; Isabel Pablos; Peter Briza; Laurian Jongejan; Neil Rigby; Juan A Asturias; Antonio Portolés; Montserrat Fernandez-Rivas; Nikolaos G Papadopoulos; Adriano Mari; Lars K Poulsen; Peter Lackner; Ronald van Ree; Fatima Ferreira; Gabriele Gadermaier Journal: Mol Nutr Food Res Date: 2019-06-26 Impact factor: 5.914
Authors: Silvia Bruznican; Hervé De Clercq; Tom Eeckhaut; Johan Van Huylenbroeck; Danny Geelen Journal: Front Plant Sci Date: 2020-01-22 Impact factor: 5.753