Bone and Joint Institute
The role of the immunoglobulin heavy chain in human anti‐dna antibody binding specificity
Document Type
Article
Publication Date
1-1-1995
Journal
Arthritis & Rheumatism
Volume
38
Issue
3
First Page
389
Last Page
395
URL with Digital Object Identifier
10.1002/art.1780380316
Abstract
Objective. To investigate the structural basis for DNA binding of the natural human IgMλ monoclonal antibody KIM4.6. Methods. An IgMλ, non–DNA‐reactive variant hybridoma was derived during in vitro subcloning of the anti‐DNA antibody KIM4.6. The variable (V)‐region heavy (H) and light (L) chain genes expressed by the variant hybridoma were amplified by polymerase chain reaction, cloned, sequenced, and compared with those of the KIM4.6 parent and other DNA‐binding and non–DNA‐binding antibodies. Results. The VL chain of the variant was identical to that of KIM4.6. In contrast, the VH chain was completely different from the VH chain of the parent but was similar or identical, except in the diversity (D) and joining regions, to the VH chain of the systemic lupus erythematosus (SLE) IgG anti‐DNA antibody T14 and SLE IgM nephritogenic anti‐DNA antibodies NE‐1 and NE‐13. Conclusion. The expression of the KIM4.6 VL chain is not sufficient for DNA specificity. The VH chain and its D region play a key role in conferring DNA binding of the KIM4.6 anti‐DNA antibody. Copyright © 1995 American College of Rheumatology
Notes
This article is freely available from the journal