کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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5915775 | 1163328 | 2010 | 4 صفحه PDF | دانلود رایگان |
Ani s 1, the major allergen of Anisakis simplex, is expected to be a useful antigen in allergen-specific immunotherapy of Anisakis allergy. To avoid side-effects such as anaphylactic shock in immunotherapy, it is desirable to use not native allergens but hypoallergenic mutants devoid of IgE-binding epitopes. This study was hence aimed to elucidate IgE-binding epitopes of Ani s 1 toward the development of hypoallergenic Ani s 1 mutants. Mapping experiments using 32 peptides (P1-32) revealed that major IgE-binding epitopes are included in P24 (region 116-130) and P28 (region 136-150). Furthermore, Ala-scanning and truncation experiments established that eight (underlined in the sequence 116-ELFAREYEGVCKSGK-130) and nine amino acid residues (underlined in the sequence 136-RGSGWMMTILGKSCD-150) are crucial for the IgE-binding of P24 and P28, respectively. The determined crucial residues of P24 and P28 were assumed to be involved in electrostatic and hydrophobic interactions with IgE, respectively.
. Ani s 1 has two IgE-binding regions (116-130 and 136-150), in which some residues are critical for IgE-binding through electrostatic or hydrophobic interaction.142Research highlightsⶠAni s 1 has two IgE-binding regions (116-130 and 136-150). ⶠEight residues in 116-130 are critical for the electrostatic binding with IgE. ⶠNine residues in 136-150 are critical for the hydrophobic binding with IgE.
Journal: Molecular and Biochemical Parasitology - Volume 174, Issue 2, December 2010, Pages 128-131