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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1984 Sep;81(18):5841–5844. doi: 10.1073/pnas.81.18.5841

Somatic mutation of the T15 heavy chain gives rise to an antibody with autoantibody specificity.

B Diamond, M D Scharff
PMCID: PMC391807  PMID: 6435121

Abstract

The S107 IgA kappa-chain myeloma cell line makes an antiphosphocholine antibody of the T15 idiotype. A somatic mutant of this line, U4, makes an immunoglobulin with a single amino acid substitution of an alanine for a glutamic acid at residue 35. This single amino acid change results in a loss of phosphocholine binding activity. However, the U4 immunoglobulin has acquired reactivity with a variety of phosphorylated macromolecules, including double-stranded DNA, protamine, and cardiolipin. Thus, a single amino acid change in the T15 heavy chain can transform an antibacterial antibody into an antibody that resembles the autoantibodies seen in mice and man with autoimmune disease.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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