Mass spectrometry-based analysis of rheumatoid factor
In summary, our findings highlight that mass spectrometry provides a platform for elucidating the heterogeneity and isotypic diversity of RF autoantibodies in RA, overcoming limitations inherent to current solid-phase RF assays. Upregulated de novo peptides were found, possibly related to the hypervariable regions of RF. Further validation using integrated proteomic and genomic approaches is required to confirm these novel peptides and their localization within the RF hypervariable regions.
Authors
- Maaike Cockx (ORCID: https://orcid.org/0000-0003-0361-5505)
- Rita Derua (ORCID: https://orcid.org/0000-0002-1784-0677)
- Sébastien Carpentier (ORCID: https://orcid.org/0000-0002-7389-6405)
- Jonas De Leeuw
- Xavier Bossuyt (ORCID: https://orcid.org/0000-0001-6856-8485)
- Doreen Dillaerts
- Tom Dehaemers (ORCID: https://orcid.org/0000-0003-4572-9383)
- Glynis Frans (ORCID: https://orcid.org/0000-0001-8528-5719)
- Patrick Verschueren (ORCID: https://orcid.org/0000-0002-0340-3580)
- Birthe Michiels (ORCID: https://orcid.org/0000-0002-3977-4172)
Institutions
- Rega Institute for Medical Research (BE)
- MRC Protein Phosphorylation and Ubiquitylation Unit (GB)
- KU Leuven (BE)
Publication Details
- Journal
- Frontiers in Immunology
- Published
- 2025-10-10
- DOI
- https://doi.org/10.3389/fimmu.2025.1644334
- Primary Topic
- Monoclonal and Polyclonal Antibodies Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00