Patient-derived monoclonal antibodies directed towards beta2 glycoprotein-1 display XXXX .

@entity1 @entity9115 @entity9500 @entity1701 @entity4555 @entity10390 @entity15327
BACKGROUND: Patients with @entity1701 ( @entity1701 ) display a heterogeneous population of antibodies with @entity9500 ) as the major antigen. OBJECTIVES: We isolated and characterized @entity1 mAbs directed against @entity9500 from the immune repertoire of @entity1701 @entity1 . METHODS: Variable heavy chain repertoires from B cells from two @entity1701 patients with anti-b(2) @entity15327 antibodies were cloned into the pHEN1-VLrep vector. Constructed full-length IgG antibodies were tested for @entity4555 ( @entity4555 ) activity and binding to @entity9500 and its domains. RESULTS: Two clones of each @entity1 were selected on the basis of the reactivity of single chain Fv ( @entity10390 ) fragments displayed on phages towards full-length @entity9500 and its isolated domain I. The affinity of selected antibodies for @entity9500 was lost when transforming from phages to monovalent scFvs, and was regained when antibodies were constructed as complete IgG, indicating a role for bivalency in binding to @entity9500 . Both selected clones from @entity1 2 recognized domain I of @entity9500 , and for both clones selected from @entity1 1, binding required the presence of both domain I and domain II. All mAbs displayed @entity4555 activity in both activated partial thromboplastin time-based and dilute @entity9115 venom test-based clotting assays and in thrombin generation. CONCLUSIONS: In this study, we show successful cloning of @entity1 -derived mAbs that require domain I of @entity9500 for binding, and that display @entity4555 activity that is dependent on their affinity for @entity9500 . These antibodies can help us to gain more insights into the pathogenesis of @entity1701 , and may facilitate standardization of @entity1701 diagnosis.
