ArticleArthritis & rheumatology (Hoboken, N.J.)2022
Antibodies to Cartilage Oligomeric Matrix Protein Are Pathogenic in Mice and May Be Clinically Relevant in Rheumatoid Arthritis.
Article in Arthritis & rheumatology (Hoboken, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
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Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it, 14 citations in OpenAlex.
- Structural and Pharmacological Network Focused on MiRNAs Involved in Rheumatoid Arthritis: A Systematic Review.Current molecular medicine · 2024Pooled it
- Protective and Pathogenic Antibodies to Citrullinated Antigens.Immunological reviews · 2026Review
- Systemic and local autoantibody responses to extracellular matrix proteins define inflammatory phenotypes across arthropathies.Rheumatology (Oxford, England) · 2026Article
- Expression profiles of miR-101-3p and miR-431-5p as potential diagnostic biomarkers for rheumatoid arthritis.Scientific reports · 2025Article
- An autoantibody profile identified by human genome-wide protein arrays in rheumatoid arthritis.MedComm · 2024Article
- Significance of Type II Collagen Posttranslational Modifications: From Autoantigenesis to Improved Diagnosis and Treatment of Rheumatoid Arthritis.International journal of molecular sciences · 2023Review
- A subset of antibodies targeting citrullinated proteins confers protection from rheumatoid arthritis.Nature communications · 2023Article
- Cartilage Oligomeric Matrix Protein, Diseases, and Therapeutic Opportunities.International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
objectiveCartilage oligomeric matrix protein (COMP) is an autoantigen in rheumatoid arthritis (RA) and experimental models of arthritis. This study was undertaken to investigate the structure, function, and relevance of anti-COMP antibodies.
methodsWe investigated the pathogenicity of monoclonal anti-COMP antibodies in mice using passive transfer experiments, and we explored the interaction of anti-COMP antibodies with cartilage using immunohistochemical staining. The interaction of the monoclonal antibody 15A11 in complex with its specific COMP epitope P6 was determined by x-ray crystallography. An enzyme-linked immunosorbent assay and a surface plasma resonance technique were used to study the modulation of calcium ion binding to 15A11. The clinical relevance and value of serum IgG specific to the COMP P6 epitope and its citrullinated variants were evaluated in a large Swedish cohort of RA patients.
resultsThe murine monoclonal anti-COMP antibody 15A11 induced arthritis in naive mice. The crystal structure of the 15A11-P6 complex explained how the antibody could bind to COMP, which can be modulated by calcium ions. Moreover, serum IgG specific to the COMP P6 peptide and its citrullinated variants was detectable at significantly higher levels in RA patients compared to healthy controls and correlated with a higher disease activity score.
conclusionOur findings provide the structural basis for binding a pathogenic anti-COMP antibody to cartilage. The recognized epitope can be citrullinated, and levels of antibodies to this epitope are elevated in RA patients and correlate with higher disease activity, implicating a pathogenic role of anti-COMP antibodies in a subset of RA patients.
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