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The major royal jelly proteins 8 and 9 ( A pi m 11) are glycosylated components of Apis mellifera venom with allergenic potential beyond carbohydrate‐based reactivity
Author(s) -
Blank S.,
Bantleon F. I.,
McIntyre M.,
Ollert M.,
Spillner E.
Publication year - 2012
Publication title -
clinical and experimental allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 154
eISSN - 1365-2222
pISSN - 0954-7894
DOI - 10.1111/j.1365-2222.2012.03966.x
Subject(s) - venom , allergen , immunology , allergy , immunoglobulin e , anaphylaxis , cross reactivity , chemistry , biology , biochemistry , antigen , antibody , cross reactions
Summary Background As hymenoptera venoms are one of the allergen sources causing the highest incidence of anaphylaxis and sometimes fatal consequences, the detailed characterization of all venom allergens is imperative for design of component‐resolved diagnostic approaches and improved intervention strategies. Objective Our aim was the immunochemical characterization of major royal jelly proteins ( MRJP ) 8 and 9, both components identified in honeybee venom ( HBV ) and putative allergens. Methods Both MRJP s were recombinantly produced as soluble differentially glycosylated proteins providing a defined degree of reactivity to cross‐reactive carbohydrate determinants ( CCD ) in insect cells. Allergen‐specific IgE (s IgE ) reactivity of HBV ‐allergic patients was analysed by ELISA and immunoblotting. Results MRJP 8 and MRJP 9 were identified as venom components by MS ‐based proteomic analyses. In a population of 47 HBV ‐allergic patients, reactivities with CCD ‐carrying MRJP s were in the range of 56% (61%), underlining the contribution of CCD s to allergen‐binding. Beyond CCD ‐reactivity, 15% of patients showed s IgE reactivity with MRJP 8 and 34% with MRJP 9 respectively. These reactivities roughly in the range of A pi m 2 render the MRJP s minor, but important allergens. Conclusion and Clinical Relevance The glycosylated MRJP 8 and MRJP 9 of HBV have IgE ‐sensitizing potential in HBV ‐allergic patients beyond CCD reactivity and have to be considered as allergens, which might be potentially important for a fraction of venom allergic patients. They are valuable tools to elucidate individual component‐resolved reactivity profiles of venom allergic patients and to provide insights into the role of particular venom components. Due to their allergenic properties, MRJP 8 and MRJP 9 were designated as isoallergens A pi m 11.0101 and A pi m 11.0201 respectively.