%0 Journal Article
%T Domain I of ¦Â2GPI is capable of blocking serum IgA antiphospholipid antibodies binding in£¿vitro: an effect enhanced by PEGylation
%A A Albay
%A A Rahman
%A B Artim-Esen
%A C Pericleous
%A C Wincup
%A I Giles
%A T McDonnell
%J Lupus
%@ 1477-0962
%D 2019
%R 10.1177/0961203319851571
%X This study aims to inhibit antiphospholipid syndrome (APS) serum derived IgA anti-beta-2-glycoprotein I (a¦Â2GPI) binding using Domain I (DI). Serum from 13 APS patients was tested for IgA a¦Â2GPI and Anti-Domain I. Whole IgA was purified by peptide M affinity chromatography from positive serum samples. Serum was tested for IgA a¦Â2GPI binding in the presence and absence of either DI or of two biochemically modified variants containing either 20£¿kDa of poly(ethylene glycol) (PEG) or 40£¿kDa of PEG. Significant inhibition with DI was possible with average inhibition of 23% (N£¿=£¿13). Further inhibitions using 20£¿kDa PEG-DI and 40£¿kDa PEG-DI variants showed significant inhibition (p£¿=£¿0.0001) with both the 40£¿kDa PEG-DI and 20£¿kDa PEG-DI variants showing increased inhibition compared with DI alone (p£¿=£¿0.0001 and p£¿=£¿0.001, n£¿=£¿10). Inhibition of IgA a¦Â2GPI by DI is possible and can be enhanced by biochemical modification in a subset of patients
%K Antiphospholipid syndrome
%K Domain I
%K PEGylation
%U https://journals.sagepub.com/doi/full/10.1177/0961203319851571