The prevalence of food allergies in the world population requires integrated approaches to identify new potential allergens, especially those of plant origin. The aim of this work was the allergen in vitro analysis of Lupinus albus seed proteome, a promising food protein source, and the assessment of IgE cross-reactivities with other more diffused legume species. A combination of one- and two-dimensional gel electrophoresis and immunoblotting analyses with specific IgGs for band identification and lupin-sensitized patients’ circulating IgEs for allergenicity studies has been used. Two lupin proteins, namely, conglutin ç and 11S globulin basic subunits, strongly reacted with all patients’ sera. Also, cross-reactivities with the homologous polypeptides of other legume species were observed. Otherwise, no reaction at all was detected with a 2S-type lupin protein. This global electrophoretic approach has allowed the identification of a new potential lupin allergen and confirmed the cross-reactivity among the legume 11S globulin basic subunits

One- and two-dimensional electrophoretic identification of IgE-binding polypeptides of lupinus albus and other legume seeds / Magni, Chiara; Herndl, Anita; Sironi, Elena; Scarafoni, Alessio; Ballabio, Cinzia; Restani, Patrizia; Bernardini, Roberto; Novembre, Elio; Vierucci, Alberto; Duranti, Marcello. - In: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. - ISSN 0021-8561. - STAMPA. - 53:(2005), pp. 4567-4571. [10.1021/jf0500785]

One- and two-dimensional electrophoretic identification of IgE-binding polypeptides of lupinus albus and other legume seeds

MAGNI, CHIARA;RESTANI, PATRIZIA;NOVEMBRE, ELIO MASSIMO;VIERUCCI, ALBERTO;
2005

Abstract

The prevalence of food allergies in the world population requires integrated approaches to identify new potential allergens, especially those of plant origin. The aim of this work was the allergen in vitro analysis of Lupinus albus seed proteome, a promising food protein source, and the assessment of IgE cross-reactivities with other more diffused legume species. A combination of one- and two-dimensional gel electrophoresis and immunoblotting analyses with specific IgGs for band identification and lupin-sensitized patients’ circulating IgEs for allergenicity studies has been used. Two lupin proteins, namely, conglutin ç and 11S globulin basic subunits, strongly reacted with all patients’ sera. Also, cross-reactivities with the homologous polypeptides of other legume species were observed. Otherwise, no reaction at all was detected with a 2S-type lupin protein. This global electrophoretic approach has allowed the identification of a new potential lupin allergen and confirmed the cross-reactivity among the legume 11S globulin basic subunits
2005
53
4567
4571
Magni, Chiara; Herndl, Anita; Sironi, Elena; Scarafoni, Alessio; Ballabio, Cinzia; Restani, Patrizia; Bernardini, Roberto; Novembre, Elio; Vierucci, Alberto; Duranti, Marcello
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1089710
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