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PDBsum entry 5jt8
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DOI no:
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Allergy
72:665-670
(2017)
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PubMed id:
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The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1.
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K.H.Meno,
J.S.Kastrup,
I.C.Kuo,
K.Y.Chua,
M.Gajhede.
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ABSTRACT
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The Blomia tropicalis (Blo t) mite species is considered a storage mite in
temperate climate zones and an important source of indoor allergens causing
allergic asthma and rhinitis in tropical and subtropical regions. Here, we
report the crystal structure of one of the allergens from Blo t, recombinant
proBlo t 1 (rproBlo t 1), determined at 2.1 Å resolution. Overall, the fold of
rproBlo t 1 is characteristic for the pro-form of cysteine proteases from the
C1A class. Structural comparison of experimentally mapped Der f 1/Der p1 IgG
epitopes to the same surface patch on Blo t 1, as well as of sequence identity
of surface-exposed residues, suggests limited cross-reactivity between these
allergens and Blo t 1. This is in agreement with ELISA inhibition results
showing that, although cross-reactive human IgE epitopes exist, there are unique
IgE epitopes for both Blo t 1 and Der p 1.
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');
}
}
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