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Remote activation of a latent epitope in an autoantigen decoded with simulated B-factors.
Front. Immunol. 10:2467 (2019)
Mutants of a catalytically inactive variant of Proteinase 3 (PR3)-iPR3-Val(103) possessing a Ser195Ala mutation relative to wild-type PR3-Val(103)-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-Val(103), a triple mutant of iPR3-Val(103), bound a monoclonal antibody (moANCA518) from a GPA patient on an epitope remote from the mutation sites, whereas the corresponding epitope of iPR3-Val(103) was latent to moANCA518. Simulated B-factor analysis revealed that the binding of moANCA518 to iHm5-Val(103) 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 center dot ANCA interactions as new GPA treatments.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Autoimmunity ; Autoantigen ; Antigenicity ; Antineutrophil Cytoplasmic Antibody ; Proteinase 3 ; B-factor; Antineutrophil Cytoplasmic Antibodies; Proteinase-3 Pr3; Wegeners-granulomatosis; Neutrophil Elastase; Molecular-dynamics; Capture-elisa; Recognition; Refinement; Interference; Restraints
ISSN (print) / ISBN
1664-3224
e-ISSN
1664-3224
Journal
Frontiers in Immunology
Quellenangaben
Volume: 10,
Article Number: 2467
Publisher
Frontiers
Publishing Place
Avenue Du Tribunal Federal 34, Lausanne, Ch-1015, Switzerland
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Lung Health and Immunity (LHI)