Why the study?
Evidence points to a link between Epstein-Barr virus and RA, prompting analysis of ACPA reactivity to citrullinated EBNA peptides to elaborate their diagnostic potential.
Do anti-citrullinated protein antibodies from rheumatoid arthritis patients react with citrullinated peptides from Epstein-Barr nuclear antigens?
Do anti-citrullinated protein antibodies from rheumatoid arthritis patients react with citrullinated peptides from Epstein-Barr nuclear antigens?
Citrullinated EBNA2 is highly reactive with RA sera, supporting its potential as a diagnostic biomarker and reinforcing the link between Epstein-Barr virus and rheumatoid arthritis onset.
Answers are grounded in this paper and cite their sources.
EBNA2 peptide reactivity may aid RA biomarker development; hypothesis-generating for EBV link, needs prospective validation.
Rheumatoid arthritis (RA) is a chronic disease which causes joint inflammation and, ultimately, erosion of the underlying bone. Diagnosis of RA is based on the presence of biomarkers, such as anti-citrullinated protein antibodies (ACPA) and rheumatoid factors, along with clinical symptoms. Much evidence points to a link between the Epstein-Barr virus and RA. In this study, we analyzed ACPA reactivity to citrullinated peptides originating from Epstein-Barr nuclear antigens (EBNA1, EBNA2, and EBNA3) in order to elaborate the diagnostic potential of citrullinated EBNA peptides. Moreover, ACPA cross-reactivity to citrullinated peptides from myelin basic protein (MBP) was analyzed, as citrullinated MBP recently was described to be associated with multiple sclerosis, and some degree of sequence homology between MBP and citrullinated EBNA exists. A peptide from EBNA2, (EBNA2-A, GQGRGRWRG-Cit-GSKGRGRMH) reacted with approximately 70% of all RA sera, whereas only limited reactivity was detected to EBNA1 and EBNA3 peptides. Moreover, screening of ACPA reactivity to hybrid peptides of EBNA3-A (EPDSRDQQS-Cit-GQRRGDENRG) and EBNA2-A and peptides containing citrulline close to the N-terminal confirmed that ACPA sera contain different populations of ACPAs. No notable ACPA reactivity to MBP peptides was found, confirming that ACPAs are specific for RA, and that other factors than the presence of a central Cit-Gly motif are crucial for antibody binding. Collectively, these findings illustrate that citrullinated EBNA2 is an optimal candidate for ACPA detection, supporting current evidence that EBV is linked to RA onset.
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Fanelli et al. (2022) studied this question.
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