ArticleResearch and practice in thrombosis and haemostasis2022
Epitope of antiphospholipid antibodies retrieved from peptide microarray based on R39-R43 of β2-glycoprotein I.
Article in Research and practice in thrombosis and haemostasis, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 6 citations in OpenAlex.
- Humoral pregnancy analyses reveal strategies for fetal protection and aberrancy in miscarriage.Cell reports. Medicine · 2026Article
- A Common Missense Variant, W335S, in β2-Glycoprotein I (APOH) is Associated with Increased Autoantibody Levels but Reduced Venous Thromboembolism Risk.medRxiv : the preprint server for health sciences · 2026Article
- Article
- The J-shape of β2GPI reveals a cryptic discontinuous epitope across domains I and II.Journal of structural biology: X · 2025Article
- Epitope of antiphospholipid antibodies retrieved from peptide microarray based on R39-R43 of β2-glycoprotein I.Research and practice in thrombosis and haemostasis · 2022Article
- Article
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Authors and funding
9 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Antiphospholipid antibody (aPL) syndrome (APS) is an autoimmune disease characterized by the presence of antiphospholipid antibodies and thromboembolic or pregnancy complications. Although cryptic epitope R39-R43 belonging to beta-2-glycoprotein 1 (β2GP1) has been identified as the main antigenic determinant for aPLs, we have recently demonstrated that the epitope is a motif determined by the polarity, rather than by the sequence or charge of amino acids. Objective: In the present study, we wanted to identify the association of residues needed to obtain the highest aPL affinity. Methods: Based on the epitope R39-R43 and our identified motif, we generated a printed peptide microarray of 676 different peptides. These peptides have been then screened for their ability to interact with the plasmas from 11 well-characterized APS patients and confirmed by surface plasma resonance assay. Results and 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.
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