Antibodies Isolated from Rheumatoid Arthritis Patients against Lysine-Containing <i>Proteus mirabilis</i> O3 (S1959) Lipopolysaccharide May React with Collagen Type I

• Main Authors: Katarzyna Durlik-Popińska, Paulina Żarnowiec, Łukasz Lechowicz, Józef Gawęda, Wiesław Kaca
• Format: Article
• Language: English
• Published: MDPI AG 2020-12-01
• Series: International Journal of Molecular Sciences
• Subjects: rheumatic diseases; rheumatoid arthritis; <i>Proteus mirabilis</i>; lipopolysaccharide; rheumatoid factor; anti-citrullinated protein antibodies
• Online Access: https://www.mdpi.com/1422-0067/21/24/9635
• ISSN: 1661-6596; 1422-0067

Most rheumatic diseases, including rheumatoid arthritis (RA), are characterized by immune disorders that affect antibody activity. In the present study, using Dot blot and ELISA assay, we showed that patients with rheumatic disease produced significantly more antibodies against lipopolysaccharide (LPS) <i>P. mirabilis</i> O3 compared to healthy donors (<i>p </i>< 0.05), and affinity purified antibodies against LPS O3 may cross-react with collagen type I. It was demonstrated that purified of antibodies isolated from RA patients sera, reacted stronger with the collagen than healthy donors (<i>p </i>= 0.015), and cross-reaction was correlated with level of anti-citrullinated peptide antibodies (r = 0.7, <i>p </i>= 0.003). Moreover, using six different lipopolysaccharides were demonstrated the significant correlations in sera reactivity among lysine-containing lipopolysaccharides observed in patients’ sera (<i>p </i>< 0.05). Using Attenuated Total Reflection Fourier Transform Infrared Spectroscopy (ATR-FTIR) it was shown that unique wavenumbers of sera spectra correlate with reactivity with lipopolysaccharides allowing distinguish patients from healthy blood donors. Antibodies adsorption by synthetic antigens shows that in patients’ group anti-LPS O3 antibodies can be adsorbed by both amides of galacturonic acid and lysine or threonine, which suggests less specificity of antibodies binding with non-carbohydrate LPS component. The observed correlations suggest that non-carbohydrate components of LPS may be an important epitope for less specific anti-LPS antibodies, which might lead to cross-reactions and affect disease development.