2S Albumin Storage Proteins: What Makes them Food Allergens?

F. Javier Moreno1, Alfonso Clemente*, 2
1 Instituto de Fermentaciones Industriales (CSIC), C/ Juan de la Cierva 3, 28006 Madrid, Spain
2 Estación Experimental del Zaidín (CSIC), Profesor Albareda 1, 18008 Granada, Spain

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2008 Bentham Science Publishers Ltd.

* Address correspondence to this author at the Estación Experimental del Zaidín (CSIC), Profesor Albareda 1, 18008 Granada, Spain; Tel: (+34) 958-572757; Fax: (+34) 958-572753; E-mail:


2S albumin storage proteins are becoming of increasing interest in nutritional and clinical studies as they have been reported as major food allergens in seeds of many mono- and di-cotyledonous plants. This review describes the main biochemical, structural and functional properties of these proteins thought to play a role in determining their potential allergenicity. 2S albumins are considered to sensitize directly via the gastrointestinal tract (GIT). The high stability of their intrinsic protein structure, dominated by a well-conserved skeleton of cysteine residues, to the harsh conditions present in the GIT suggests that these proteins are able to cross the gut mucosal barrier to sensitize the mucosal immune system and/or elicit an allergic response. The flexible and solvent-exposed hypervariable region of these proteins is immunodominant and has the ability to bind IgE from allergic patients´ sera. Several linear IgE-binding epitopes of 2S albumins spanning this region have been described to play a major role in allergenicity; the role of conformational epitopes of these proteins in food allergy is far from being understood and need to be investigated. Finally, the interaction of these proteins with other components of the food matrix might influence the absorption rates of immunologically reactive 2S albumins but also in their immune response.

Keywords: 2S albumins, food allergy, IgE-binding proteins, epitope mapping, disulphide bonds.