Cross-reactivity of a human IgG1 anticitrullinated fibrinogen monoclonal antibody to a citrullinated profilaggrin peptide
Identifieur interne : 000735 ( Main/Exploration ); précédent : 000734; suivant : 000736Cross-reactivity of a human IgG1 anticitrullinated fibrinogen monoclonal antibody to a citrullinated profilaggrin peptide
Auteurs : Nicole Hartwig Trier [Danemark] ; Maria Louise Leth [Danemark] ; Paul Robert Hansen [Danemark] ; Gunnar Houen [Danemark]Source :
- Protein Science : A Publication of the Protein Society [ 0961-8368 ] ; 2012.
Abstract
Rheumatoid arthritis (RA) is the most common autoimmune rheumatic disease. It is characterized by persistent joint inflammation, resulting in loss of joint function, morbidity and premature mortality. The presence of antibodies against citrullinated proteins is a characteristic feature of RA and up to 70% of RA patients are anticitrullinated protein antibody (ACPA) positive. ACPA responses have been widely studied and are suggested to be heterogeneous, favoring antibody cross-reactivity to citrullinated proteins. In this study, we examined factors that may influence cross-reactivity between a commercial human anticitrullinated fibrinogen monoclonal antibody and a citrullinated peptide. Using a citrullinated profilaggrin sequence (HQCHQEST- Cit-GRSRGRCGRSGS) as template, cyclic and linear truncated peptide versions were tested for reactivity to the monoclonal antibody. Factors such as structure, peptide length and flanking amino acids were found to have a notable impact on antibody cross-reactivity. The results achieved contribute to the understanding of the interactions between citrullinated peptides and ACPA, which may aid in the development of improved diagnostics of ACPA.
Url:
DOI: 10.1002/pro.2178
PubMed: 23076998
PubMed Central: 3575922
Affiliations:
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Ø</wicri:regionArea></affiliation></author><author><name sortKey="Houen, Gunnar" sort="Houen, Gunnar" uniqKey="Houen G" first="Gunnar" last="Houen">Gunnar Houen</name><affiliation wicri:level="1"><nlm:aff id="au1"><institution>Department of Clinical Biochemistry, Immunology and Genetics, Statens Serum Institut</institution><addr-line>Artillerivej 5, 2300 Copenhagen S, Denmark</addr-line></nlm:aff><country xml:lang="fr">Danemark</country><wicri:regionArea>Artillerivej 5, 2300 Copenhagen S</wicri:regionArea><wicri:noRegion>2300 Copenhagen S</wicri:noRegion></affiliation></author></analytic><series><title level="j">Protein Science : A Publication of the Protein Society</title><idno type="ISSN">0961-8368</idno><idno type="eISSN">1469-896X</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Rheumatoid arthritis (RA) is the most common 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It is characterized by persistent joint inflammation, resulting in loss of joint function, morbidity and premature mortality. The presence of antibodies against citrullinated proteins is a characteristic feature of RA and up to 70% of RA patients are anticitrullinated protein antibody (ACPA) positive. ACPA responses have been widely studied and are suggested to be heterogeneous, favoring antibody cross-reactivity to citrullinated proteins. In this study, we examined factors that may influence cross-reactivity between a commercial human anticitrullinated fibrinogen monoclonal antibody and a citrullinated peptide. Using a citrullinated profilaggrin sequence (HQCHQEST- Cit-GRSRGRCGRSGS) as template, cyclic and linear truncated peptide versions were tested for reactivity to the monoclonal antibody. Factors such as structure, peptide length and flanking amino acids were found to have a notable impact on antibody cross-reactivity. 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