Figure 8.
Figure 8. Mechanism describing the binding of antiphospholipid antibodies toβ2-GPI. Our proposed mechanism is based on our findings in this study together with both the crystal structure and the NMR structure of β2-GPI in solution: (1) Antiphos-pholipid antibodies cannot bind β2-GPI in solution because epitope G40-R43 is covered by one of the carbohydrate chains. (2) Binding to a phospholipid membrane induces a conformational change in β2-GPI. (3) As a result, the carbohydrate chain is not able to cover epitope G40-R43 anymore and is now able to bind antiphospholipid antibodies.

Mechanism describing the binding of antiphospholipid antibodies toβ2-GPI. Our proposed mechanism is based on our findings in this study together with both the crystal structure and the NMR structure of β2-GPI in solution: (1) Antiphos-pholipid antibodies cannot bind β2-GPI in solution because epitope G40-R43 is covered by one of the carbohydrate chains. (2) Binding to a phospholipid membrane induces a conformational change in β2-GPI. (3) As a result, the carbohydrate chain is not able to cover epitope G40-R43 anymore and is now able to bind antiphospholipid antibodies.

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