ArticleRheumatology (Oxford, England)2024
The central helicase domain holds the major conformational epitopes of melanoma differentiation-associated gene 5 autoantibodies.
Article in Rheumatology (Oxford, England), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Dermatomyositis with Anti-MDA5 Autoantibodies After SARS-CoV-2 mRNA Vaccination Treated with Tofacitinib: Integrating Literature Evidence and a Novel Observation.Antibodies (Basel, Switzerland) · 2026Review
- Pathogenesis and Treatment of Interstitial Lung Disease Accompanied by Anti-melanoma Differentiation-associated Gene 5-positive Idiopathic Inflammatory Myopathies.Internal medicine (Tokyo, Japan) · 2026Review
- Anti- Melanoma Differentiation-Associated Gene 5 Antibody Positive Dermatomyositis: Recent Progress in Pathophysiology and Treatment.Current rheumatology reports · 2025Review
- Comprehensive Enteroviral Serology Links Infection and Anti-Melanoma Differentiation-Associated Protein 5 Dermatomyositis.ACR open rheumatology · 2025Article
- When viral infections meet the anti-MDA5 antibody-positive dermatomyositis.Frontiers in immunology · 2025Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
objectiveAutoantibodies against MDA5 (melanoma differentiation-associated protein 5) serve as a biomarker for DM (dermatomyositis) and indicate a risk factor for interstitial lung disease (ILD). MDA5 is a protein responsible for sensing RNA virus infection and activating signalling pathways against it. However, little is known about the antigen epitopes on MDA5 autoantibodies. We aimed to determine the interaction of the MDA5 autoantibody-antigen epitope.
methodsCell-based assays (CBAs), immunoprecipitation-immunoblot assays, and various immunoblotting techniques were used in the study.
resultsWe demonstrated that DM patient autoantibodies recognize MDA5 epitopes in a native conformation-dependent manner. Furthermore, we identified the central helicase domain （3Hel） formed by Hel1, Hel2i, Hel2, and pincer as the major epitopes. As proof of principle, the purified 3Hel efficiently absorbed MDA5 autoantibodies from patient sera through immunoprecipitation-immunoblot assay.
conclusionOur study uncovered the nature of the antigen epitopes on MDA5 and can provide guidance for diagnosis and a targeted therapeutic approach development.
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