Phage antibodies: filamentous phage displaying antibody variable domains

@article{McCafferty1990PhageAF,
  title={Phage antibodies: filamentous phage displaying antibody variable domains},
  author={John McCafferty and Andrew D. Griffiths and Gregory Paul Winter and D. J. Chiswell},
  journal={Nature},
  year={1990},
  volume={348},
  pages={552-554}
}
NEW ways of making antibodies have recently been demonstrated using gene technology. Immunoglobulm 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 (see ref. 1 for review). Screening of V genes would, however, be revolutionized if they could be expressed on the surface of bacteriophage. Phage carrying V genes that encode… Expand
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References

SHOWING 1-10 OF 18 REFERENCES
Antibody-selectable filamentous fd phage vectors: affinity purification of target genes.
TLDR
Fusion-phage vectors that accept foreign DNA inserts with little effect on phage function are introduced; affinity purification of virions bearing a target determinant from a 10(8)-fold excess of phage not bearing the determinant is described, using minute amounts of antibody. Expand
Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
TLDR
Isolated variable domains may offer an alternative to monoclonal antibodies and serve as the key to building high-affinity human antibodies and the name 'single domain antibodies (dAbs)' is suggested for these antigen binding demands. Expand
Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface.
Foreign DNA fragments can be inserted into filamentous phage gene III to create a fusion protein with the foreign sequence in the middle. The fusion protein is incorporated into the virion, whichExpand
Searching for peptide ligands with an epitope library.
Tens of millions of short peptides can be easily surveyed for tight binding to an antibody, receptor or other binding protein using an "epitope library." The library is a vast mixture of filamentousExpand
A new filamentous phage cloning vector: fd-tet.
TLDR
This new phage, fd-tet, may be used as a cloning vector to produce large quantities of cloned DNA in single-stranded form and its usefulness has been demonstrated by cloning of a fragment from bacteriophage lambda. Expand
Cloning immunoglobulin variable domains for expression by the polymerase chain reaction.
TLDR
A set of oligonucleotide primers designed to amplify the cDNA of mouse immunoglobulin heavy and light chain variable domains by the polymerase chain reaction are applied to clone and sequence the variable domains of five hybridoma antibodies and to express a mouse-human chimeric antibody that binds to the human mammary carcinoma line MCF-7. Expand
Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda.
A novel bacteriophage lambda vector system was used to express in Escherichia coli a combinatorial library of Fab fragments of the mouse antibody repertoire. The system allows rapid and easyExpand
Random peptide libraries: a source of specific protein binding molecules.
TLDR
This type of library makes it possible to identify peptides that bind to proteins (or other macromolecules) that have no previously known affinity for peptides. Expand
Human monoclonals from antigen-specific selection of B lymphocytes and transformation by EBV.
TLDR
By this method, monoclonal antibodies to both foreign antigens and autoantigens can be prepared from the normal human B-cell repertoire. Expand
Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli.
  • J. Huston, D. Levinson, +7 authors R. Crea
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1988
A biosynthetic antibody binding site, which incorporated the variable domains of anti-digoxin monoclonal antibody 26-10 in a single polypeptide chain (Mr = 26,354), was produced in Escherichia coliExpand
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