Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes
Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes
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DOI:
10.1016/j.imlet.2005.03.014
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发表时间:
2005-09-15
影响因子:
4.4
通讯作者:
Rougé, P
中科院分区:
文献类型:
--
作者:
Barre, A;Borges, JP;Rougé, P
Three-dimensional models built for the peanut Ara h 2 allergen and other structurally-related 2S albumin allergens of dietary nuts exhibited an overall three-dimensional fold stabilized by disulphide bridges well conserved among all the members of the 2S albumin superfamily. Conformational analysis of the linear IgE-binding epitopes mapped on the molecular surface of Ara h 2 showed no structural homology with the corresponding regions of the walnut Jug r 1, the pecan nut Car i 1 or the Brazil nut Ber e 1 allergens. The absence of epitopic community does not support the allergenic cross-reactivity observed between peanut and walnut or Brazil nut, which presumably depends on other ubiquitous seed storage protein allergens, namely the vicilins. However, the major IgE-binding epitope identified on the molecular surface of the walnut Jug r 1 allergen shared a pronounced structural homology with the corresponding region of the pecan nut Car i I allergen. With the exception of peanut, 2S albumins could thus account for the IgE-binding cross-reactivity observed between some other dietary nuts, e.g. walnut and pecan nut. (c) 2005 Elsevier B.V. All rights reserved.