ArticleScientific reports2021
Specific domain V reduction of beta-2-glycoprotein I induces protein flexibility and alters pathogenic antibody binding.
Article in Scientific reports, 2021. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Molecular dynamics simulations of beta-2-glycoprotein 1 (β2GPI) reveal that post-translational modifications facilitate novel structures.Scientific reports · 2026Article
- Antiphospholipid Syndrome-Diagnostic and Methodologic Approach.Metabolites · 2025Review
- The absence of standardization in antiphospholipid antibody testing may favor the use of 99th percentile cutoffs in antiphospholipid syndrome classification.Research and practice in thrombosis and haemostasis · 2025Article
- Understanding the structure of βBlood vessels, thrombosis & hemostasis · 2025Review
- Cysteine and methionine oxidation in thrombotic disorders.Current opinion in chemical biology · 2023Review
- Article
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Authors and funding
12 authors at 5 institutions in 4 countries.
Funding
Abstract
Beta-2-glycoprotein I (β2GPI) is a blood protein and the major antigen in the autoimmune disorder antiphospholipid syndrome (APS). β2GPI exists mainly in closed or open conformations and comprises of 11 disulfides distributed across five domains. The terminal Cys288/Cys326 disulfide bond at domain V has been associated with different cysteine redox states. The role of this disulfide bond in conformational dynamics of this protein has not been investigated so far. Here, we report on the enzymatic driven reduction by thioredoxin-1 (recycled by Tris(2-carboxyethyl)phosphine; TCEP) of β2GPI. Specific reduction was demonstrated by Western blot and mass spectrometry analyses confirming majority targeting to the fifth domain of β2GPI. Atomic force microscopy images suggested that reduced β2GPI shows a slightly higher proportion of open conformation and is more flexible compared to the untreated protein as confirmed by modelling studies. We have determined a strong increase in the binding of pathogenic APS autoantibodies to reduced β2GPI as demonstrated by ELISA. Our study is relevant for understanding the effect of β2GPI reduction on the protein structure and its implications for antibody binding in APS patients.
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Registered trials
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