Cardiolipin interacts with beta-2-glycoprotein I and forms an open conformation-Mechanisms analyzed using hydrogen/deuterium exchange.

ABSTRACT: Beta-2-glycoprotein I (β₂ GPI) is the major antigen for the antiphospholipid antibodies in the antiphospholipid syndrome. The exposed epitope in domain I of β₂ GPI can be recognized by the anti-β₂ GPI antibody. Here, we prepared the anionic di-oleoyl-phosphatidylserine (DOPS) and cardiolipin (CL) liposomes to interact with the β₂ GPI. The conformational changes of β₂ GPI upon binding with the liposomes were analyzed using hydrogen/deuterium exchange mass spectrometry. The exchange level of sequences 21-27 significantly increased after β₂ GPI had interacted with DOPS. This change indicated a reduced interaction between domain I and domain V, inferring to a protrusion of the sequences 21-27 from the ring conformation. After β<

SUBMITTER: Tang KT 

PROVIDER: S-EPMC8040858 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature