Metal-binding chimeric antibodies expressed in Escherichia coli

Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9754-8. doi: 10.1073/pnas.89.20.9754.

Abstract

Metallothionein, a well-characterized biological chelator of metals, has been genetically fused to the binding domain of an antibody and expressed in the periplasm of Escherichia coli. Specific delivery of 109Cd to immobilized hapten or to haptenated cells was demonstrated directly in periplasmic extracts. This approach is potentially useful for targeted radiotherapy and diagnostic imaging. We find six to seven atoms of metal per active antigen-combining site. Absence of the Fc portion of the immunoglobulin along with low immunogenicity of metallothionein-metal complexes should reduce immunologic reactions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / chemistry*
  • Base Sequence
  • Cadmium Radioisotopes / metabolism
  • Escherichia coli
  • Gene Expression
  • Haptens / metabolism
  • Melanoma, Experimental
  • Metallothionein / chemistry*
  • Molecular Sequence Data
  • Nitrohydroxyiodophenylacetate
  • Radionuclide Imaging / methods
  • Rats
  • Recombinant Fusion Proteins / chemistry*
  • Tumor Cells, Cultured

Substances

  • Antibodies, Monoclonal
  • Cadmium Radioisotopes
  • Haptens
  • Recombinant Fusion Proteins
  • Nitrohydroxyiodophenylacetate
  • Metallothionein