A genetically encoded direct sensor of antibody-antigen interactions

Chembiochem. 2009 Sep 4;10(13):2162-4. doi: 10.1002/cbic.200900254.

Abstract

To overcome the limitations imposed by the genetic code on the engineering of proteins with new or enhanced physical, chemical, or biological properties, we developed a general method for the site specific incorporation of unnatural amino acids into proteins directly in living cells.[1] An orthogonal tRNA/aminoacyl-tRNA synthetase pair (one that does not crossreact with host tRNAs and aminoacyl-tRNA synthetases) is evolved to deliver a specific non-natural amino acid into a protein in response to a nonsense or frameshift codon. To date, we have selectively incorporated over 40 unnatural amino acids into a diverse set of proteins in both prokaryotic and eukaryotic organisms using this methodology.[2]

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Antibodies / immunology
  • CD40 Ligand / chemistry*
  • CD40 Ligand / immunology*
  • Fluorescent Dyes / chemistry
  • Immunoglobulin Fab Fragments / chemistry*
  • Immunoglobulin Fab Fragments / genetics*
  • Immunoglobulin Fab Fragments / immunology
  • Protein Binding
  • Spectrometry, Fluorescence
  • Umbelliferones / chemistry*
  • Umbelliferones / metabolism

Substances

  • Antibodies
  • Fluorescent Dyes
  • Immunoglobulin Fab Fragments
  • Umbelliferones
  • CD40 Ligand
  • 7-hydroxycoumarin