Molecular cloning, expression, and chromosome 19 localization of a human Ro/SS-A autoantigen.

D P McCauliffe; F A Lux; T S Lieu; I Sanz; J Hanke; M M Newkirk; L L Bachinski; Y Itoh; M J Siciliano; M Reichlin

doi:10.1172/JCI114582

Department of Dermatology, University of Texas, Southwestern Medical Center, Dallas 75238.

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Department of Dermatology, University of Texas, Southwestern Medical Center, Dallas 75238.

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Department of Dermatology, University of Texas, Southwestern Medical Center, Dallas 75238.

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Department of Dermatology, University of Texas, Southwestern Medical Center, Dallas 75238.

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Department of Dermatology, University of Texas, Southwestern Medical Center, Dallas 75238.

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Department of Dermatology, University of Texas, Southwestern Medical Center, Dallas 75238.

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Department of Dermatology, University of Texas, Southwestern Medical Center, Dallas 75238.

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Department of Dermatology, University of Texas, Southwestern Medical Center, Dallas 75238.

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Department of Dermatology, University of Texas, Southwestern Medical Center, Dallas 75238.

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Department of Dermatology, University of Texas, Southwestern Medical Center, Dallas 75238.

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Published in Volume 85, Issue 5 on May 1, 1990
J Clin Invest. 1990;85(5):1379–1391. https://doi.org/10.1172/JCI114582.
© 1990 The American Society for Clinical Investigation

Published May 1, 1990 - Version history

Ro/SS-A antibodies are found in a number of human autoimmune disorders including Sjogren's syndrome and several systemic lupus erythematosus-related disorders. These heterogeneous autoantibodies are known to recognize several distinct cellular antigens. With synthetic oligonucleotides corresponding to amino acid sequence information we have isolated a full-length cDNA clone which encodes a human Ro ribonucleoprotein autoantigen. The 1,890-base pair clone contains an open reading frame that encodes a 417-amino acid, 48-kD polypeptide that migrates aberrantly at 60 kD by SDS-PAGE. Rabbit antibodies raised against this protein's recently described amino-terminal epitope react with a previously identified 52-kD human Ro protein and immunoprecipitate the human cytoplasmic RNAs. Ultraviolet light cross-linking studies suggest that this Ro protein binds each of the four major human cytoplasmic RNAs. The deduced amino acid sequence is 63% homologous to an Onchocerca volvulus antigen. Southern filter hybridization analysis indicates that this gene is not highly polymorphic and exists as a single copy in the human genome. Chromosomal localization studies place this gene on the short arm of chromosome 19 near the gene encoding the low density lipoprotein receptor.

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