Phage display of functional, full-length human and viral membrane proteins

Bioorg Med Chem Lett. 2008 Nov 15;18(22):5937-40. doi: 10.1016/j.bmcl.2008.07.051. Epub 2008 Jul 17.

Abstract

Phage display of protein and peptide libraries offers a powerful technology for the selection and isolation of ligands and receptors. To date, the technique has been considered limited to soluble, non-membrane proteins. We report two examples of phage display of full-length, folded and functional membrane proteins. Consistent display required the recently reported KO7(+) helper phage. The two proteins, full-length caveolin-1 and HIV gp41, display well on the surface of the phage, and maintain their binding activities as shown by in vitro assays.

Publication types

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

MeSH terms

  • Bacteriophages / chemistry
  • Caveolin 1 / chemistry
  • Caveolin 1 / metabolism
  • HIV Envelope Protein gp41 / chemistry
  • HIV Envelope Protein gp41 / metabolism
  • Humans
  • Membrane Proteins / chemistry*
  • Membrane Proteins / immunology
  • Membrane Proteins / metabolism
  • Models, Molecular*
  • Peptide Library
  • Structure-Activity Relationship
  • Viral Matrix Proteins / chemistry*
  • Viral Matrix Proteins / immunology
  • Viral Matrix Proteins / metabolism

Substances

  • Caveolin 1
  • HIV Envelope Protein gp41
  • Membrane Proteins
  • Peptide Library
  • Viral Matrix Proteins
  • gp41 protein, Human immunodeficiency virus 1