The J-shape of β2GPI reveals a cryptic discontinuous epitope across domains I and II.

ABSTRACT: Beta-2-Glycoprotein I is the main target for pathogenic antiphospholipid syndrome autoantibodies. It can adopt several conformations, including an O-shape and two more linear J- and S-shapes. The in vivo existence of the O-shape is debated, and doubt remains pertaining to the pathogenic impact of each shape. Studies have shown that APS antibodies react weakly with the O-shape and bind to the linear shapes due to the exposure of a cryptic epitope in the 1st domain. How the protein transitions from O-shape to the linear shapes remains unknown. While the main epitope is widely recognised as the R39-R43 peptide, there is evidence pointing to a discontinuous epitope across domains I and II (DI & DII). We used molecular dynamics simulations to examine the potential pathways of conformatio

SUBMITTER: Lalaurie CJ 

PROVIDER: S-EPMC12398265 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature