Introduction
Specificity of Antiphospholipid Antibodies
Binding of Anti-domain I Antibodies to β2GPI Is Conformation Dependent
Association Between Anti-domain I Antibodies and Clinical Symptoms
Domain I as Clinical Drug
Conclusions
Anti-domain I assay | Anti-β2GPI ELISA | |
---|---|---|
Conformation of β2GPI | Conformation independent, as only domain I is coated | Binding of antibodies to β2GPI depends on whether epitope R39–R43 is exposed |
Charge of the ELISA plate | A neutral plate is needed to prevent epitope R39–R43 from being coated downward to the plate | A negative plate is needed, which is thought to induce a conformational change and enables 1 antibody to bind 2 molecules |
Specificity and sensitivity | High specificity, but it is not known whether other pathogenic antibody populations are missed | High sensitivity, but a mediocre specificity, as a significant number of positive patients do not develop APS-related clinical symptoms |
Source of protein | Domain I is produced and thereby recombinant | β2GPI can be purified from human or bovine plasma, or produced recombinant. It is not known whether there are differences in conformation between the different sources |
Purification | Domain I contains a his-tag and is purified via nickel-Sepharosea
| β2GPI can be purified by applying different techniques; the influence of the different techniques on the conformation of β2GPI is not known |