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• W2982077892 abstract "Mutants of a catalytically inactive variant of Proteinase 3 (PR3)—iPR3-Val103 possessing a Ser195Ala mutation relative to wild-type PR3-Val103—offer insights into how autoantigen PR3 interacts with antineutrophil cytoplasmic antibodies (ANCAs) in granulomatosis with polyangiitis (GPA) and whether such interactions can be interrupted. Here we report that iHm5-Val103, a triple mutant of iPR3-Val103, bound a monoclonal antibody (moANCA518) from a GPA patient on an epitope remote from the mutation sites, whereas the corresponding epitope of iPR3-Val103 was latent to moANCA518. Simulated B-factor analysis revealed that the binding of moANCA518 to iHm5-Val103 was due to increased main-chain flexibility of the latent epitope caused by remote mutations, suggesting rigidification of epitopes with therapeutics to alter pathogenic PR3•ANCA interactions as new GPA treatments." @default.
• W2982077892 created "2019-11-01" @default.
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• W2982077892 date "2019-10-25" @default.
• W2982077892 modified "2023-10-17" @default.
• W2982077892 title "Remote Activation of a Latent Epitope in an Autoantigen Decoded With Simulated B-Factors" @default.
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• W2982077892 doi "https://doi.org/10.3389/fimmu.2019.02467" @default.
• W2982077892 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6823208" @default.
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