Epitope of antiphospholipid antibodies retrieved from peptide microarray based on R39-R43 of β2-glycoprotein I

CONCLUSIONS: We identified a peptide that selectively bound immunoglobulin G (IgG) derived from APS patients with 100 times more affinity than β2GP1, Domain I, or epitope R39-R43. This peptide is able to inhibit the activity of IgG derived from APS patients in vitro. We have also generated a monoclonal IgG antibody against this peptide. Using both peptide and monoclonal antibody, we have been able to develop a fully standardized indirect colorimetric immunoassay with highly sensitivity. The identification of the optimized peptide offers a new standardized and accurate tool for diagnostics of APS. Furthermore, having increased affinity for aPL, this peptide could represent a useful tool as prevention strategy for APS and an alternative to the use of anticoagulants.PMID:36304483 | PMC:PMC9592562 | DOI:10.1002/rth2.12828

Source: Thrombosis and Haemostasis - October 28, 2022 Category: Hematology Authors: Marc Moghbel Aline Roth Daniela Baptista Kapka Miteva Fabienne Burger Fabrizio Montecucco Nicolas Vuilleumier Fran çois Mach Karim J Brandt Source Type: research