| Literature DB >> 2247164 |
J McCafferty1, A D Griffiths, G Winter, D J Chiswell.
Abstract
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.Entities:
Mesh:
Substances:
Year: 1990 PMID: 2247164 DOI: 10.1038/348552a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962