Pre-existing anti-drug antibodies in Fabry disease show less affinity for pegunigalsidase alfa
Malte Lenders, Solvey Pollmann, Melina Terlinden, Eva Brand
Abstract
: 2.18 ± 1.51 μmol) (both p < 0.0001). Cross-ELISAs supported the presence of masked epitopes on PRX-102. Importantly, inhibition measurements also revealed a 30% reduction in inhibitory capacity of pre-existing ADAs towards PRX-102. Enzyme-uptake experiments in AGAL-deficient EA.hy926 cells demonstrated less effects of ADAs on cellular PRX-102 uptake compared with agalsidase beta. We conclude that due to the reduced affinity of pre-existing ADAs against agalsidase-alfa or -beta, ADA-affected patients might benefit from a therapy switch to PRX-102, which is currently evaluated in clinical trials.
Topics & Concepts
AntibodyChemistryPEGylationFabry diseaseEpitopeEnzymeRecombinant DNAPharmacologyBETA (programming language)Internal medicineMedicineEndocrinologyMolecular biologyDiseaseBiochemistryImmunologyBiologyGeneProgramming languagePolyethylene glycolComputer scienceLysosomal Storage Disorders ResearchTrypanosoma species research and implicationsCarbohydrate Chemistry and Synthesis