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Research Article Free access | 10.1172/JCI115968

Autoantibodies against the amino-terminal cadherin-like binding domain of pemphigus vulgaris antigen are pathogenic.

M Amagai, S Karpati, R Prussick, V Klaus-Kovtun, and J R Stanley

Dermatology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.

Find articles by Amagai, M. in: PubMed | Google Scholar

Dermatology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.

Find articles by Karpati, S. in: PubMed | Google Scholar

Dermatology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.

Find articles by Prussick, R. in: PubMed | Google Scholar

Dermatology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.

Find articles by Klaus-Kovtun, V. in: PubMed | Google Scholar

Dermatology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.

Find articles by Stanley, J. in: PubMed | Google Scholar

Published September 1, 1992 - More info

Published in Volume 90, Issue 3 on September 1, 1992
J Clin Invest. 1992;90(3):919–926. https://doi.org/10.1172/JCI115968.
© 1992 The American Society for Clinical Investigation
Published September 1, 1992 - Version history
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Abstract

Complementary DNA cloning of the 130-kD pemphigus vulgaris (PV) autoantigen (PVA) has indicated that it is a member of the cadherin family of Ca(2+)-dependent cell adhesion molecules. By homology with typical cadherins, PVA has five extracellular domains (EC1 through EC5). To localize immunogenic domains and to determine whether antibodies against them might be pathogenic, we produced beta-galactosidase fusion proteins with cDNA encoding different portions of the extracellular domains of PVA (EC1-2, EC3-5, and each individual domain). Immunoblot analysis of these fusion proteins with 23 PV patients' sera demonstrated that major immunogenic regions of PVA are located on the EC1, EC2, and EC4 domains. IgG was affinity-purified from PV sera on fusion proteins representing the amino (EC1-2) and carboxy (EC3-5) terminus of the extracellular PVA, and injected into neonatal mice. PV IgG affinity-purified on the EC1-2 fusion protein caused suprabasilar acantholysis, the typical histological finding of PV, but IgG affinity-purified on the EC3-5 fusion protein or beta-galactosidase alone did not. These results indicate that at least one pathogenic epitope, which is sufficient to cause suprabasilar acantholysis in neonatal mice, is located on the amino-terminal region of PVA, an area thought to be important in cadherin homophilic adhesion.

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