{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T23:33:29Z","timestamp":1782862409264,"version":"3.54.5"},"reference-count":54,"publisher":"American Society of Hematology","issue":"26","content-domain":{"domain":["ashpublications.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2025,12,25]]},"abstract":"<jats:sec>\n                    <jats:title>Abstract<\/jats:title>\n                    <jats:p>Antiphospholipid antibodies targeting \u03b22-glycoprotein I (\u03b22GPI) are a hallmark of antiphospholipid syndrome (APS), associated with an increased risk of thrombosis and pregnancy morbidity. Among these, antibodies targeting domain I (DI) are common in individuals at higher risk; however, their epitopes and prevalence among APS phenotypes remain unclear. Here, we use a large collection of 29 structurally and functionally validated \u03b22GPI variants to provide new insights into the molecular mechanisms of autoantibody recognition in APS. Using the prototypic human-derived monoclonal anti-DI antibody MBB2, we identified positively charged residue R39 as the key driver of MBB2 binding, followed by residues R43, N56, and T57. Structural analyses revealed that although R39 is solvent exposed, R43 is not, because it is caged by residues N56 and T57. The narrow epitope footprint explains why MBB2 exhibits a modest affinity for soluble \u03b22GPI. The cage structure accounts for the epitope being conformational rather than linear. Mutational analyses of immunoglobulin G anti-\u03b22GPI antibodies from 52 patients with triple-positive APS, 37 with a history of thrombosis and 15 nonvascular obstetric patients, confirmed significant reactivity against DI and showed signatures of 2 conformational epitopes: one similar to MBB2 (epitope I), in which the presence of R39 is essential, and another that does not require R39 (epitope II). Although less frequent than epitope II in our cohort, epitope I reactivity was notably enriched in patients with vascular-obstetric APS. Varying epitope specificities for DI may therefore aid in identifying different APS phenotypes and predicting clinical outcomes.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1182\/blood.2025029488","type":"journal-article","created":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T20:04:26Z","timestamp":1759349066000},"page":"3234-3245","update-policy":"https:\/\/doi.org\/10.1182\/blood.2019cm0000","source":"Crossref","is-referenced-by-count":7,"title":["Domain and residue mapping of autoantibodies to \u03b22GPI reveals differences among antiphospholipid syndrome phenotypes"],"prefix":"10.1182","volume":"146","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0710-2520","authenticated-orcid":false,"given":"Suresh","family":"Kumar","sequence":"first","affiliation":[{"name":"1Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0007-2933-1961","authenticated-orcid":false,"given":"Deepesh","family":"Vaid","sequence":"additional","affiliation":[{"name":"1Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7987-9497","authenticated-orcid":false,"given":"Paola","family":"Lonati","sequence":"additional","affiliation":[{"name":"2Laboratory of Immunorheumatologic Researches, IRCCS Istituto Auxologico Italiano, Milan, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0796-7535","authenticated-orcid":false,"given":"Arianna","family":"Da Via","sequence":"additional","affiliation":[{"name":"2Laboratory of Immunorheumatologic Researches, IRCCS Istituto Auxologico Italiano, Milan, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marta","family":"Tonello","sequence":"additional","affiliation":[{"name":"3Rheumatology Section, Department of Medicine, University of Padua, Padua, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3394-1451","authenticated-orcid":false,"given":"Pier Luigi","family":"Meroni","sequence":"additional","affiliation":[{"name":"2Laboratory of Immunorheumatologic Researches, IRCCS Istituto Auxologico Italiano, Milan, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vittorio","family":"Pengo","sequence":"additional","affiliation":[{"name":"4Thrombosis Research Laboratory, Department of Cardio-Thoracic, Vascular Sciences, and Public Health, University of Padua, Padua, Italy"},{"name":"5Arianna Foundation on Anticoagulation, Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2309-7100","authenticated-orcid":false,"given":"Nicola","family":"Pozzi","sequence":"additional","affiliation":[{"name":"1Edward A. 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