Plasmin cleavage of β2-glycoprotein I alters its structure and ability to bind to pathogenic antibodies

Cleavage of β2GPI by plasmin results in the production of a unique S-shaped structural conformation and higher patient antibody binding. This novel structure may increase the production of antibodies and explain the loss of binding to phospholipids described previously for plasmin-clipped β2GPI.

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Publication Details

Journal
Journal of Thrombosis and Haemostasis
Published
2025-02-24
DOI
https://doi.org/10.1016/j.jtha.2025.02.015
Citations
3
Primary Topic
Protease and Inhibitor Mechanisms
Type
article
Field-Weighted Citation Impact
2.81

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article

Plasmin cleavage of β2-glycoprotein I alters its structure and ability to bind to pathogenic antibodies

Paul A. Dalby, Hannah M. Britt, Thomas McDonnell, Christophe J. Lalaurie et al.
3 citations
Journal of Thrombosis and Haemostasis
Protease and Inhibitor Mechanisms
2.81
article

Plasmin cleavage of β2-glycoprotein I alters its structure and ability to bind to pathogenic antibodies

Paul A. Dalby, Hannah M. Britt, Thomas McDonnell, Christophe J. Lalaurie, Konstantinos Thalassinos, Anisur Rahman, Ian Giles, Hannah F. Bradford, Mihaela Delcea, Stephen J. Perkins, Xin Gao, Jayesh Gor, Charis Pericleous
article en
3 citations

Abstract

Cleavage of β2GPI by plasmin results in the production of a unique S-shaped structural conformation and higher patient antibody binding. This novel structure may increase the production of antibodies and explain the loss of binding to phospholipids described previously for plasmin-clipped β2GPI.

Journal of Thrombosis and HaemostasisVol. 23(6)
Biochemical Society (GB), The Royal Free Hospital (GB), Universität Greifswald (DE), Institute of Structural and Molecular Biology (GB), Institute of Infection and Immunity (CA), University College London (GB), Imperial College London (GB)
Wellcome Trust, Versus Arthritis, Engineering and Physical Sciences Research Council, Medical Research Foundation
Zero hunger
Openalex Percentile: Top 11%
Protease and Inhibitor Mechanisms
2.81
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