Specific labeling of cell surface proteins with chemically diverse compounds

J Am Chem Soc. 2004 Jul 28;126(29):8896-7. doi: 10.1021/ja048396s.

Abstract

The specific and covalent labeling of fusion proteins with synthetic molecules opens up new ways to study protein function in the living cell. Here we present a novel method that allows for the specific and exclusive extracellular labeling of proteins on the surfaces of live cells with a large variety of synthetic molecules including fluorophores, protein ligands, or quantum dots. The approach is based on the specific labeling of fusion proteins of acyl carrier protein with synthetic molecules through post-translational modification catalyzed by phosphopantetheine transferase. The specificity and versatility of the labeling should allow it to become an important tool for studying and manipulating cell surface proteins and for complementing existing approaches in cell surface engineering.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Carrier Protein / chemistry*
  • Acyl Carrier Protein / metabolism
  • Biotinylation
  • Coenzyme A / chemistry*
  • Coenzyme A / metabolism
  • Membrane Proteins / analysis*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Receptors, Cell Surface / analysis
  • Receptors, Cell Surface / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Transferases (Other Substituted Phosphate Groups) / chemistry
  • Transferases (Other Substituted Phosphate Groups) / metabolism

Substances

  • Acyl Carrier Protein
  • Membrane Proteins
  • Receptors, Cell Surface
  • Recombinant Proteins
  • Transferases (Other Substituted Phosphate Groups)
  • holo-(acyl-carrier-protein) synthase
  • Coenzyme A