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Efficient phage display of polypeptides fused to the carboxy‐terminus of the M13 gene‐3 minor coat protein
Author(s) -
Fuh Germaine,
Sidhu Sachdev S.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01946-3
Subject(s) - phage display , linker , phagemid , fusion protein , complementary dna , coat protein , gene , microbiology and biotechnology , biology , n terminus , chemistry , biochemistry , peptide sequence , bacteriophage , recombinant dna , peptide , computer science , rna , escherichia coli , operating system
We report that, contrary to common belief, polypeptides fused to the carboxy‐terminus of the M13 gene‐3 minor coat protein are functionally displayed on the phage surface. In a phagemid display system, carboxy‐terminal fusion through optimized linker sequences resulted in display levels comparable to those achieved with conventional amino‐terminal fusions. These findings are of considerable importance to phage display technology because they enable investigations not suited to amino‐terminal display, including the study of protein–protein interactions requiring free carboxy‐termini, functional cDNA cloning efforts, and the display of intracellular proteins.