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Unlocking the allergenic structure of the major house dust mite allergen Der f 2 by elimination of key intramolecular interactions
Author(s) -
Takai Toshiro,
Ichikawa Saori,
Yokota Toyokazu,
Hatanaka Hideki,
Inagaki Fuyuhiko,
Okumura Yasushi
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02096-2
Subject(s) - intramolecular force , allergen , chemistry , house dust mite , histamine , immunoglobulin e , circular dichroism , mite , epitope , conformational change , sensitization , stereochemistry , allergy , immunology , antibody , biology , pharmacology , botany
We report on the structural background of the remarkable reduction of allergenicity in engineering of the major house dust mite allergen Der f 2. Disruption of intramolecular disulfide bonds in Der f 2 caused extensive conformational change that was monitored by circular dichroism and gel‐filtration analysis. The degree of conformational change correlated well with the degree of reductions in the capacity to bind IgE and to induce histamine release from basophils in mite‐allergic patients. Loosening the rigid tertiary structure by elimination of key intramolecular interactions is an effective strategy to reduce the number of high affinity IgE epitopes of allergen vaccine.