{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T13:02:11Z","timestamp":1790600531239,"version":"4.1.0"},"reference-count":52,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2026,2,17]],"date-time":"2026-02-17T00:00:00Z","timestamp":1771286400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"},{"start":{"date-parts":[[2026,2,17]],"date-time":"2026-02-17T00:00:00Z","timestamp":1771286400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Allergy"],"published-print":{"date-parts":[[2026,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>Peanut allergy is a serious form of food allergy that can lead to anaphylactic reactions. Research has shown that the Ara h 2 allergen is immunodominant and associated with fatal systemic reactions.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>We determined the crystal structure of recombinant Ara h 2.0201 in a complex with the human\u2010derived PA12P3D08 (D08) IgE Fab fragment at 3.2\u2009\u00c5 resolution. In addition, native mass spectrometry was used to study interactions of D08 with Ara h 2 and its peptides.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>The structure revealed that D08 Fab binds to a long loop of Ara h 2.0201, which contains three repeated DPYSPS motifs. The immunocomplex structure illustrated how three copies of D08 Fabs can bind simultaneously to Ara h 2.0201 in close proximity. Native mass spectrometry studies of D08 Fab with Ara h 2.0201 and peptides containing 2\u20133 motifs demonstrated cross\u2010linking of Ara h 2.0201 in solution and the propensity of D08 Fab to self\u2010associate. Motif peptides from Ara h 2.0201 highlighted the importance of proline hydroxylation for binding affinity. D08 Fab also bound to hydroxyproline\u2010containing peptides from Ara h 1 and 3.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>The trivalent binding is effective in forming large allergen\u2010IgE complexes on mast cell or basophil surfaces and contributes to the potency of Ara h 2 in triggering allergic reactions and highlighting its role in anaphylaxis. Proline hydroxylation considerably enhances D08 binding affinity and contributes to cross\u2010reactivity among Ara h 1\u20133 allergens.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/all.70258","type":"journal-article","created":{"date-parts":[[2026,2,17]],"date-time":"2026-02-17T08:40:40Z","timestamp":1771317640000},"page":"2036-2046","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Structural Basis for Trivalent Cross\u2010Linking of a Patient\u2010Derived\n                    <scp>IgE<\/scp>\n                    Antibody by the Major Peanut Allergen Ara h 2.0201"],"prefix":"10.1111","volume":"81","author":[{"given":"Tarja","family":"Parkkinen","sequence":"first","affiliation":[{"name":"Department of Chemistry and Sustainable Technology University of Eastern Finland  Joensuu 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