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.
journal_name
Front Immunoljournal_title
Frontiers in immunologyauthors
Pang YP,Casal Moura M,Thompson GE,Nelson DR,Hummel AM,Jenne DE,Emerling D,Volkmuth W,Robinson WH,Specks Udoi
10.3389/fimmu.2019.02467subject
Has Abstractpub_date
2019-10-25 00:00:00pages
2467issn
1664-3224journal_volume
10pub_type
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pub_type: 杂志文章,评审
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