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Bead Arrays for Antibody and Complement Profiling Reveal Joint Contribution of Antibody Isotypes to C3 Deposition
KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology.ORCID iD: 0000-0001-7843-2960
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2014 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 9, no 5, e96403- p.Article in journal (Refereed) Published
Abstract [en]

The development of antigen arrays has provided researchers with great tools to identify reactivities against self or foreign antigens from body fluids. Yet, these approaches mostly do not address antibody isotypes and their effector functions even though these are key points for a more detailed understanding of disease processes. Here, we present a bead array-based assay for a multiplexed determination of antigen-specific antibody levels in parallel with their properties for complement activation. We measured the deposition of C3 fragments from serum samples to reflect the degree of complement activation via all three complement activation pathways. We utilized the assay on a bead array containing native and citrullinated peptide antigens to investigate the levels of IgG, IgM and IgA autoantibodies along with their complement activating properties in serum samples of 41 rheumatoid arthritis patients and 40 controls. Our analysis revealed significantly higher IgG reactivity against the citrullinated fibrinogen beta and filaggrin peptides as well as an IgA reactivity that was exclusive for citrullinated fibrinogen b peptide and C3 deposition in rheumatoid arthritis patients. In addition, we characterized the humoral immune response against the viral EBNA-1 antigen to demonstrate the applicability of this assay beyond autoimmune conditions. We observed that particular buffer compositions were demanded for separate measurement of antibody reactivity and complement activation, as detection of antigen-antibody complexes appeared to be masked due to C3 deposition. We also found that rheumatoid factors of IgM isotype altered C3 deposition and introduced false-positive reactivities against EBNA-1 antigen. In conclusion, the presented bead-based assay setup can be utilized to profile antibody reactivities and immune-complex induced complement activation in a high-throughput manner and could facilitate the understanding and diagnosis of several diseases where complement activation plays role in the pathomechanism.

Place, publisher, year, edition, pages
2014. Vol. 9, no 5, e96403- p.
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:kth:diva-147429DOI: 10.1371/journal.pone.0096403ISI: 000336656000073Scopus ID: 2-s2.0-84900387101OAI: oai:DiVA.org:kth-147429DiVA: diva2:731001
Funder
Science for Life Laboratory - a national resource center for high-throughput molecular bioscience
Note

QC 20140630

Available from: 2014-06-30 Created: 2014-06-27 Last updated: 2017-12-05Bibliographically approved
In thesis
1. Affinity Arrays for Profiling Proteins and Autoantibody Repertoires
Open this publication in new window or tab >>Affinity Arrays for Profiling Proteins and Autoantibody Repertoires
2014 (English)Doctoral thesis, comprehensive summary (Other academic)
Place, publisher, year, edition, pages
Stockholm: KTH Royal Institute of Technology, 2014. xi, 159 p.
Series
TRITA-BIO-Report, ISSN 1654-2312 ; 2014:12
National Category
Biomedical Laboratory Science/Technology
Identifiers
urn:nbn:se:kth:diva-150398 (URN)978-91-7595-209-3 (ISBN)
Public defence
2014-09-05, Inghesalen, Karolinska Institute, Tomtebodavägen 18 A, Solna, 10:00 (English)
Opponent
Supervisors
Funder
Science for Life Laboratory - a national resource center for high-throughput molecular bioscience
Note

QC 20140902

Available from: 2014-09-02 Created: 2014-09-02 Last updated: 2014-09-02Bibliographically approved

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Ayoglu, Burcu

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