Anti-Mi2 autoantibodies target plant homeodomain (PHD) fingers of SP140L and TIF1γ, while anti-TIF1γ autoantibodies primarily bind TIF1γ outside the PHD region
Authors' conclusion
Anti-Mi2 autoantibodies recognize the PHD fingers of SP140L and TIF1γ. TIF1γ is recognized by two different myositis-specific autoantibodies: anti-Mi2 autoantibodies bind the C-terminal PHD domain and anti-TIF1γ autoantibodies predominantly bind the N-terminal region.
Study context
- Population
- Serum samples from myositis patients, disease controls and healthy controls
- Outcome
- Autoantibody recognition of SP140L and TIF1γ fragments (LIPS)
Methodological detailsLuciferase immunoprecipitation system (LIPS) assays
- LIPS assays
Main finding
As reported in the abstract
- Anti-Mi2 autoantibodies recognised SP140L; a 49 amino acid PHD finger fragment of SP140L increased specificity for selectively detecting anti-Mi2
- Anti-Mi2 autoantibodies weakly bound TIF1γ compared with anti-TIF1γ autoantibodies
- Excluding the TIF1γ PHD finger eliminated cross-reactivity with anti-Mi2 autoantibodies
- Switching two amino acids in the TIF1γ PHD finger to resemble AIRE markedly enhanced anti-Mi2 immunoreactivity
- Anti-TIF1γ autoantibodies primarily recognised the N-terminal fragment outside the PHD finger (immunodominant epitopes)
Original publication
Anti-Mi2 autoantibodies target PHD fingers of SP140L and TIF1γ, while anti-TIF1γ autoantibodies primarily bind TIF1γ outside the PHD region. Rheumatology (Oxford). Published 6 August 2025. doi:10.
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