ArticleWorld journal of gastroenterology2010
Catalytic domain of PDC-E2 contains epitopes recognized by antimitochondrial antibodies in primary biliary cirrhosis.
Article in World journal of gastroenterology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- A Review of Therapies for Primary Biliary Cholangitis.Gastroenterology & hepatology · 2026Article
- SARS-CoV-2 Gut-Targeted Epitopes: Sequence Similarity and Cross-Reactivity Join Together for Molecular Mimicry.Biomedicines · 2023Article
- Challenges and opportunities in achieving effective regulatory T cell therapy in autoimmune liver disease.Seminars in immunopathology · 2022Review
- Antigen presentation, autoantibody production, and therapeutic targets in autoimmune liver disease.Cellular & molecular immunology · 2021Review
- Antibodies to the Muscarinic Acetylcholine Receptor M3 in Primary Biliary Cholangitis Inhibit Receptor Function on Cholangiocytes.Frontiers in immunology · 2020Article
- Burden of Primary Biliary Cholangitis Among Inpatient Population in the United States.Hepatology communications · 2019Article
- Sulphite oxidase (SO) - a mitochondrial autoantigen as target for humoral and cellular immune reactions in primary sclerosing cholangitis.BMC gastroenterology · 2018Article
- Autoantibodies in Autoimmune Liver Disease-Clinical and Diagnostic Relevance.Frontiers in immunology · 2018Review
- Primary biliary cirrhosis: Clinical and laboratory criteria for its diagnosis.World journal of gastroenterology · 2015Review
- The autoimmunity of primary biliary cirrhosis and the clonal selection theory.Immunology and cell biology · 2011Review
- Human SepSecS or SLA/LP: selenocysteine formation and autoimmune hepatitis.Biological chemistry · 2010Review
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Authors and funding
5 authors.
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Abstract
aimTo search for further immunodominant peptides of the pyruvate dehydrogenase complex E2-component (PDC-E2) recognized by antimitochondrial antibodies (AMA) in primary biliary cirrhosis (PBC).
methodsSera from 95 patients with PBC were tested by enzyme-linked immunosorbent assay against 33 synthetic overlapping peptides (25 amino acids; aa) covering the entire length of the E2-subunit of PDC-E2. Furthermore, the inner lipoyl peptide 167-184 was used in an unlipoylated and a lipoylated form as well as coupled to ovalbumin. Sera from 11 AMA negative/ANA positive PBC patients, 63 patients with other liver disorders and 22 healthy blood donors served as controls.
resultsOf the 95 PBC-sera, 74% reacted with the peptide 475-499 and 58% with the peptide 407-431 located within the catalytic domain of PDC-E2. Patients with other disorders or healthy controls were positive in only up to 18%. Antibodies to the unlipoylated and lipoylated peptide 167-184 within the inner lipoyl domain were found in only 5% and 11% of the PBC sera, respectively; using ovalbumin-coupled peptides, the incidence increased up to 57% (unlipoylated form).
conclusionPeptides within the catalytic site of PDC-E2 rather than the previously reported lipoyl binding peptide 167-184 may represent major immunodominant epitopes recognized by AMA in PBC.
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