Phage display of functional, full-length human and viral membrane proteins.
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.
Majumdar
Sudipta
S
Department of Chemistry, University of California, Irvine, CA 92697, USA.
Hajduczki
Agnes
A
Mendez
Aaron S
AS
Weiss
Gregory A
GA
D001435:Bacteriophages / Q000737:chemistry; D051242:Caveolin 1 / Q000737:chemistry / Q000378:metabolism; D015700:HIV Envelope Protein gp41 / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D008958:Models, Molecular; D019151:Peptide Library; D013329:Structure-Activity Relationship; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism
D051242:Caveolin 1; D015700:HIV Envelope Protein gp41; D008565:Membrane Proteins; D019151:Peptide Library; D014763:Viral Matrix Proteins; C514787:gp41 protein, Human immunodeficiency virus 1