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.

Full Text

Duke Authors

Cited Authors

  • Pisetsky, DS; Grudier, JP

Published Date

  • December 1, 1989

Published In

Volume / Issue

  • 143 / 11

Start / End Page

  • 3609 - 3613

PubMed ID

  • 2511245

International Standard Serial Number (ISSN)

  • 0022-1767


  • eng

Conference Location

  • United States