Polyspecific binding of Escherichia coli beta-galactosidase by murine antibodies to DNA.
Journal Article (Journal Article)
To characterize further polyspecific interactions of antibodies to DNA, the binding of sera from autoimmune MRL-lpr/lpr mice to Escherichia coli beta-galactosidase (beta-gal) was analyzed. This protein was selected for study because of preliminary observations that sera from autoimmune mice bound unexpectedly to cloned fusion protein constructions containing beta-gal. Using ELISA assays, sera from MRL-lpr/lpr mice demonstrated high levels of antibodies to both DNA and beta-gal, in titers significantly greater than those of BALB/c controls. Affinity chromatography using beta-gal-Sepharose demonstrated that antibodies enriched for anti-beta-gal activity bound both DNA as well as beta-gal, indicating the presence of a population of cross-reactive anti-DNA antibodies. Furthermore, anti-DNA mAb of MRL-lpr/lpr strain origin also bound beta-gal by ELISA, although these levels were lower than those to DNA. Together, these results extend the range of polyspecific binding of murine anti-DNA antibodies to bacterial proteins. They further suggest caution in the interpretation of immunoassays using fusion protein constructions containing beta-gal, especially with sera from autoimmune mice.
- Pisetsky, DS; Grudier, JP
- December 1, 1989
Volume / Issue
- 143 / 11
Start / End Page
- 3609 - 3613
International Standard Serial Number (ISSN)
- United States