Antibodies Isolated from Rheumatoid Arthritis Patients against Lysine-Containing <i>Proteus mirabilis</i> O3 (S1959) Lipopolysaccharide May React with Collagen Type I
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 (L...
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doaj-f46b72d82a7c418d9f0465a83f4ad5822020-12-18T00:04:55ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-12-01219635963510.3390/ijms21249635Antibodies Isolated from Rheumatoid Arthritis Patients against Lysine-Containing <i>Proteus mirabilis</i> O3 (S1959) Lipopolysaccharide May React with Collagen Type IKatarzyna Durlik-Popińska0Paulina Żarnowiec1Łukasz Lechowicz2Józef Gawęda3Wiesław Kaca4Department of Microbiology and Parasitology, Institute of Biology, Jan Kochanowski University, 25-369 Kielce, PolandDepartment of Microbiology and Parasitology, Institute of Biology, Jan Kochanowski University, 25-369 Kielce, PolandDepartment of Microbiology and Parasitology, Institute of Biology, Jan Kochanowski University, 25-369 Kielce, PolandRheumatology Clinic ARTIMED, 25-022 Kielce, PolandDepartment of Microbiology and Parasitology, Institute of Biology, Jan Kochanowski University, 25-369 Kielce, PolandMost 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.https://www.mdpi.com/1422-0067/21/24/9635rheumatic diseasesrheumatoid arthritis<i>Proteus mirabilis</i>lipopolysacchariderheumatoid factoranti-citrullinated protein antibodies |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Katarzyna Durlik-Popińska Paulina Żarnowiec Łukasz Lechowicz Józef Gawęda Wiesław Kaca |
spellingShingle |
Katarzyna Durlik-Popińska Paulina Żarnowiec Łukasz Lechowicz Józef Gawęda Wiesław Kaca Antibodies Isolated from Rheumatoid Arthritis Patients against Lysine-Containing <i>Proteus mirabilis</i> O3 (S1959) Lipopolysaccharide May React with Collagen Type I International Journal of Molecular Sciences rheumatic diseases rheumatoid arthritis <i>Proteus mirabilis</i> lipopolysaccharide rheumatoid factor anti-citrullinated protein antibodies |
author_facet |
Katarzyna Durlik-Popińska Paulina Żarnowiec Łukasz Lechowicz Józef Gawęda Wiesław Kaca |
author_sort |
Katarzyna Durlik-Popińska |
title |
Antibodies Isolated from Rheumatoid Arthritis Patients against Lysine-Containing <i>Proteus mirabilis</i> O3 (S1959) Lipopolysaccharide May React with Collagen Type I |
title_short |
Antibodies Isolated from Rheumatoid Arthritis Patients against Lysine-Containing <i>Proteus mirabilis</i> O3 (S1959) Lipopolysaccharide May React with Collagen Type I |
title_full |
Antibodies Isolated from Rheumatoid Arthritis Patients against Lysine-Containing <i>Proteus mirabilis</i> O3 (S1959) Lipopolysaccharide May React with Collagen Type I |
title_fullStr |
Antibodies Isolated from Rheumatoid Arthritis Patients against Lysine-Containing <i>Proteus mirabilis</i> O3 (S1959) Lipopolysaccharide May React with Collagen Type I |
title_full_unstemmed |
Antibodies Isolated from Rheumatoid Arthritis Patients against Lysine-Containing <i>Proteus mirabilis</i> O3 (S1959) Lipopolysaccharide May React with Collagen Type I |
title_sort |
antibodies isolated from rheumatoid arthritis patients against lysine-containing <i>proteus mirabilis</i> o3 (s1959) lipopolysaccharide may react with collagen type i |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2020-12-01 |
description |
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. |
topic |
rheumatic diseases rheumatoid arthritis <i>Proteus mirabilis</i> lipopolysaccharide rheumatoid factor anti-citrullinated protein antibodies |
url |
https://www.mdpi.com/1422-0067/21/24/9635 |
work_keys_str_mv |
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