NDLI: Reactivity of primary biliary cirrhosis sera with Escherichia coli dihydrolipoamide acetyltransferase (E2p): characterization of the main immunogenic region.

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Reactivity of primary biliary cirrhosis sera with Escherichia coli dihydrolipoamide acetyltransferase (E2p): characterization of the main immunogenic region.

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Reactivity of primary biliary cirrhosis sera with Escherichia coli dihydrolipoamide acetyltransferase (E2p): characterization of the main immunogenic region.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	James, O. F. Ali, S. T. Guest, J. R. Bassendine, M. F. Fussey, S. P. Yeaman, S. J.
Description	Author Affiliation: Fussey SP ( Department of Biochemistry, Medical School, University of Newcastle upon Tyne, United Kingdom.);
Abstract	Primary biliary cirrhosis (PBC) is a chronic cholestatic liver disease characterized by the presence of antimitochondrial autoantibodies in the serum. The major antigens recognized by the antibodies are the E2 components of the 2-oxo acid dehydrogenase complexes, all of which possess covalently attached lipoic acid cofactors. A bacterial etiology has been proposed for the disease, and patients' antibodies are known to recognize the E2 subunits (E2p) of both mammalian and bacterial pyruvate dehydrogenase complexes. Immunoblotting and ELISA inhibition techniques using extracts of Escherichia coli deletion strains, genetically restructured E2 polypeptides, and isolated lipoyl domains demonstrate that (i) the E2o subunit of the E. coli 2-oxoglutarate dehydrogenase complex is recognized by patients' antibodies; (ii) the main immunogenic region of E2p lies within the lipoly domains; (iii) the presence of a lipoly residue within the domain is crucial for effective recognition by the antibodies; and (iv) octanoylated E2p, octanoylated E2o, and octanoylated lipoyl domain, produced by a mutant deficient in lipoate biosynthesis, are recognized by patients' antibodies but not as effectively as their lipoylated counterparts. These findings indicate that antibodies in PBC patients' sera bind to a unique peptide-cofactor conformation within the lipoyl domains of the E2 polypeptides and that this epitope is partially mimicked by substituting the lipoyl cofactor with an octanoyl group.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	87
Language	English
Publisher	National Academy of Sciences
Publisher Date	1990-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetyltransferases Immunology Autoantibodies Isolation & Purification Liver Cirrhosis, Biliary Amino Acid Sequence Antigen-Antibody Complex Antigen-Antibody Reactions Dihydrolipoyllysine-Residue Acetyltransferase Enzyme-Linked Immunosorbent Assay Escherichia Coli Enzymology Immunoblotting Ketoglutarate Dehydrogenase Complex Blood Macromolecular Substances Mitochondria, Liver Molecular Sequence Data Pyruvate Dehydrogenase Complex Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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