Autoantibody to DNA excision repair enzyme hMYH in a patient with rheumatic disease

Clinical Immunology : the Official Journal of the Clinical Immunology Society
F P LaiB H Toh

Abstract

We screened a human HepG2 cell cDNA expression library using serum from a patient with rheumatic disease. This serum had immunofluorescence reactivity to nuclei with a homogeneous staining pattern and to punctuate nuclear aggregates, chromosomal metaphase plate, midbody, and cytoplasmic bridge. YT1, the longest cDNA clone isolated, has sequence identity to hMYH, the human homologue of the Escherichia coli excision repair enzyme, DNA adenine glycosylase MutY. YT1 is a truncated cDNA of 1619 bp, encoding amino acids 22-535, and contains a full-length 3'-UTR sequence. We were unable to express a bacterial malE fusion protein incorporating amino acids 22 to 535 of hMYH. Consequently, we generated two additional malE fusion proteins of hMYH encoding amino acids 1-120 (pMAL-c2:hMYH(1-120)) and amino acids 121-535 (pMAL-c2:hMYH(121-535)). The patient serum immunoblotted only pMAL-c2:hMYH(1-120), suggesting that the autoepitope(s) is restricted to amino acids 22-120 of hMYH, and detected a protein of approximately 59-kDa in total HeLa and nuclear extracts consistent with reactivity to hMYH. Affinity-purified autoantibodies to pMAL-c2:hMYH(1-120) reacted by immunoblot to pMAL-c2:hMYH(1-120), with no reactivity to pMAL-c2:hMYH(121-535). ...Continue Reading

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Citations

Jun 3, 2021·International Journal of Molecular Sciences·Theodora ManolakouDimitrios T Boumpas

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