Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: Dihydrolipoamide acetyltransferase

R. L. Coppel, L. J. McNeilage, C. D. Surh, J. Van De Water, T. W. Spithill, S. Whittingham, M. E. Gershwin

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Abstract

Primary biliary cirrhosis is a chronic, destructive autoimmune liver disease of humans. Patient sera are characterized by a high frequency (> 95%) of autoantibodies to a M(r) 70,000 mitochondrial antigen, a component of the M2 antigen complex. We have identified a human cDNA clone encoding the complete amino acid sequence of this autoantigen. The predicted structure has significant similarity with the dihydrolipoamide acetyltransferase (EC 2.3.1.12) of the Escherichia coli pyruvate dehydrogenase multienzyme complex. The human sequence preserves the Glu-Thr-Asp-Lys-Ala motif of the lipoyl-binding site and has two potential binding sites. Expressed fragments of the cDNA react strongly with sera from patients with primary biliary cirrhosis but not with sera from patients with autoimmune chronic acxtive hepatitis or sera from healthy subjects.

Original languageEnglish
Pages (from-to)7317-7321
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number19
DOIs
Publication statusPublished - 1 Jan 1988
Externally publishedYes

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