{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,7]],"date-time":"2026-06-07T16:37:31Z","timestamp":1780850251531,"version":"3.54.1"},"reference-count":36,"publisher":"American Society of Hematology","issue":"12","content-domain":{"domain":["ashpublications.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2023,3,23]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>von Willebrand factor (VWF) is a multimeric protein, the size of which is regulated via ADAMTS13-mediated proteolysis within the A2 domain. We aimed to isolate nanobodies distinguishing between proteolyzed and non-proteolyzed VWF, leading to the identification of a nanobody (designated KB-VWF-D3.1) targeting the A3 domain, the epitope of which overlaps the collagen-binding site. Although KB-VWF-D3.1 binds with similar efficiency to dimeric and multimeric derivatives of VWF, binding to VWF was lost upon proteolysis by ADAMTS13, suggesting that proteolysis in the A2 domain modulates exposure of its epitope in the A3 domain. We therefore used KB-VWF-D3.1 to monitor VWF degradation in plasma samples. Spiking experiments showed that a loss of 10% intact VWF could be detected using this nanobody. By comparing plasma from volunteers to that from congenital von Willebrand disease (VWD) patients, intact-VWF levels were significantly reduced for all VWD types, and most severely in VWD type 2A\u2013group 2, in which mutations promote ADAMTS13-mediated proteolysis. Unexpectedly, we also observed increased proteolysis in some patients with VWD type 1 and VWD type 2M. A significant correlation (r\u00a0= 0.51, P\u00a0&amp;lt; .0001) between the relative amount of high\u2013molecular weight multimers and levels of intact VWF was observed. Reduced levels of intact VWF were further found in plasmas from patients with severe aortic stenosis and patients receiving mechanical circulatory support. KB-VWF-D3.1 is thus a nanobody that detects changes in the exposure of its epitope within the collagen-binding site of the A3 domain. In view of its unique characteristics, it has the potential to be used as a diagnostic tool to investigate whether a loss of larger multimers is due to ADAMTS13-mediated proteolysis.<\/jats:p>","DOI":"10.1182\/blood.2022017569","type":"journal-article","created":{"date-parts":[[2022,12,24]],"date-time":"2022-12-24T00:36:35Z","timestamp":1671842195000},"page":"1457-1468","update-policy":"https:\/\/doi.org\/10.1182\/blood.2019cm0000","source":"Crossref","is-referenced-by-count":6,"title":["A nanobody against the VWF A3 domain detects ADAMTS13-induced proteolysis in congenital and\u00a0acquired VWD"],"prefix":"10.1182","volume":"141","author":[{"given":"Claire","family":"Kizlik-Masson","sequence":"first","affiliation":[{"name":"1Laboratory for Hemostasis, Inflammation & Thrombosis, Unit\u00e9 Mixte de Recherche 1176, Institut National de la Sant\u00e9 et de la Recherche M\u00e9dicale, Universit\u00e9 Paris-Saclay, Le Kremlin-Bic\u00eatre, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3843-642X","authenticated-orcid":false,"given":"Ivan","family":"Peyron","sequence":"additional","affiliation":[{"name":"1Laboratory for Hemostasis, Inflammation & Thrombosis, Unit\u00e9 Mixte de Recherche 1176, Institut National de la Sant\u00e9 et de la Recherche M\u00e9dicale, Universit\u00e9 Paris-Saclay, Le Kremlin-Bic\u00eatre, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"St\u00e9phane","family":"Gangnard","sequence":"additional","affiliation":[{"name":"1Laboratory for Hemostasis, Inflammation & Thrombosis, Unit\u00e9 Mixte de Recherche 1176, Institut National de la Sant\u00e9 et de la Recherche M\u00e9dicale, Universit\u00e9 Paris-Saclay, Le Kremlin-Bic\u00eatre, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gaelle","family":"Le Goff","sequence":"additional","affiliation":[{"name":"2Diagnostica Stago, Unit\u00e9s de recherche 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