Biochemical and immunochemical characterization of hop-hornbeam (Ostrya Carpinifolia Scop.) pollen |
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Authors: | Stefania Patriarca Susanna Voltolini Riccardo Navone Stefania Martini Carlo Montanari A Negrini Elisabetta Cosulich |
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Institution: | (1) Centro Biotecnologie Avanzate, Genova, Italy;(2) Azienda Ospedaliera San Martino, Genova, Italy;(3) Dip.per lo studio del Territorio e delle sue Risorse Corso Europa, 26 I-16132 Genova;(4) Dipartimento di Biochimica, Pavia, Italy |
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Abstract: | In the last few years Ostrya carpinifolia pollen is consideredas an important cause of respiratoryallergy in Mediterranean areas. The concentration ofthe pollen was measured over a period of fifteen yearsfrom 1981 to 1996 in an area around Genoa; the resultsof this study have clearly indicated an increasingtrend that correlate with persons sensitization.In this study we sought to define the immunochemical andbiochemical properties of hop-hornbean pollen. Soluble proteins extracted from Ostryacarpinifolia pollen and from the taxonomicallyrelated species Corylus Avellana, were analyzedby polyacrylamide gel electrophoresis (SDS-PAGE), byhorizontal isoelectrofocusing (IEF) and by twodimensions electrophoresis (2D-PAGE). Allergenicproteins were identified with sera of sensibilizedpatients and cross-reactivity was evaluated byimmunoblotting techniques. The electrophoreticanalysis showed a partial identity between theproteins from Ostrya and Corylus extracts. The immunoblotting assay, developed withhuman IgE from subjects allergic to hop-hornbeampollen, displayed the major IgE reactivity for acomponent with a molecular weight of 17 kDa expressedin both Ostrya and Corylus extracts. This reactivity is consistent with the presence ofBet v 1 that is described as the major pollen allergenin the Betulaceae and Corylaceae families. Sera fromsubjects allergic to Ostrya were then preadsorbed with recombinant Bet v 1 immobilized in the Pharmacia CAP System; a significant reduction ofthe IgE binding activity was observed after thetreatment. We therefore suggest that Bet v 1 couldbe one of the allergenic proteins present in theOstrya pollen possibly being responsible forcross-reactivity with other members of taxonomicallyrelated families. |
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Keywords: | allergens blotting inhibition Corylus avellana cross-reactivity IgE Ostrya carpinifolia 2D-PAGE |
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