Phage antibodies: filamentous phage displaying antibody variable domains.
New ways of making antibodies have recently been demonstrated using gene technology. Immunoglobulin variable (V) genes are amplified from hybridomas or B cells using the polymerase chain reaction, and cloned into expression vectors. Soluble antibody fragments secreted from bacteria are then screened for binding activities. Screening of V genes would, however, be revolutionized if they could be expressed on the surface of bacteriophage. Phage carrying V genes that encode binding activities could then be selected directly with antigen. Here we show that complete antibody V domains can be displayed on the surface of fd bacteriophage, that the phage bind specifically to antigen and that rare phage (one in a million) can be isolated after affinity chromatography.
McCafferty
J
J
MRC Laboratory of Molecular Biology, Cambridge, UK.
Griffiths
A D
AD
Winter
G
G
Chiswell
D J
DJ
D000595:Amino Acid Sequence; D000906:Antibodies / Q000235:genetics*; D001483:Base Sequence; D002846:Chromatography, Affinity; D003001:Cloning, Molecular / Q000379:methods; D003090:Coliphages / Q000235:genetics*; D005803:Genes, Immunoglobulin; D005822:Genetic Vectors; D007135:Immunoglobulin Variable Region / Q000235:genetics*; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes
D000906:Antibodies; D007135:Immunoglobulin Variable Region; D015345:Oligonucleotide Probes