Literature DB >> 2247164

Phage antibodies: filamentous phage displaying antibody variable domains.

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.

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Year:  1990        PMID: 2247164     DOI: 10.1038/348552a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  479 in total

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7.  Phage antibodies neutralize vaccinia virus.

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8.  The rational design of a 'type 88' genetically stable peptide display vector in the filamentous bacteriophage fd.

Authors:  D Enshell-Seijffers; L Smelyanski; J M Gershoni
Journal:  Nucleic Acids Res       Date:  2001-05-15       Impact factor: 16.971

9.  Vibrio cholerae hemagglutinin/protease inactivates CTXphi.

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10.  Human monoclonal antibodies against a plethora of viral pathogens from single combinatorial libraries.

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