Evidence map›Paper›PMID 12239343›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

A method for the generation of combinatorial antibody libraries using pIX phage display.

Changshou Gao, Shenlan Mao, Gunnar Kaufmann, Peter Wirsching, Richard A Lerner, Kim D Janda

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

45 citing papers in PubMed.

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  12. Chicken antibodies against venom proteins ofThe journal of venomous animals and toxins including tropical diseases · 2020
    Article
  13. Review
  14. Review
  15. Generating FN3-Based Affinity Reagents Through Phage Display.Current protocols in chemical biology · 2018
    Article
  16. Review
  17. Review
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Changshou GaoDepartment of Chemistry, The Scripps Research Institute and The Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Shenlan Mao
Gunnar Kaufmann
Peter Wirsching
Richard A Lerner
Kim D Janda

Funding

TUMORICIDAL ACTIVITY OF HOST COMPLEMENTP01CA027489 · NCI · SCRIPPS RESEARCH INSTITUTE · PI LERNER, RICHARD ALAN · 1985 to 2004
$7.7M
NCI NIH HHS P01 CA027489NCI NIH HHS P01CA27489
6 · The paper itself

Abstract

For more than a decade, phage displayed combinatorial antibody libraries have been used to generate and select a wide variety of antibodies. We previously reported that the phage coat proteins pVII and pIX could be used to display the heterodimeric structure of the antibody Fv region. Herein, aspects of this technology were invoked and extended to construct a large, human single-chain Fv (scFv) library of 4.5 x 10(9) members displayed on pIX of filamentous bacteriophage. Furthermore, the diversity, quality, and utility of the library were demonstrated by the selection of scFv clones against six different protein antigens. Notably, more than 90% of the selected clones showed positive binding for their respective antigens after as few as three rounds of panning. Analyzed scFvs were also found to be of high affinity. For example, kinetic analysis (BIAcore) revealed that scFvs against staphylococcal enterotoxin B and cholera toxin B subunit had a nanomolar and subnanomolar dissociation constant, respectively, affording affinities comparable to, or exceeding that, of mAbs obtained from immunization. High specificity was also attained, not only between very distinct proteins, but also in the case of the Ricinus communis ("ricin") agglutinins (RCA(60) and RCA(120)), despite >80% sequence homology between the two. The results suggested that the performance of pIX-display libraries can potentially exceed that of the pIII-display format and make it ideally suited for panning a wide variety of target antigens.

Indexed as

Peptide LibraryBacteriophagesDNA, ComplementaryEnzyme-Linked Immunosorbent AssayHumansImmunoglobulin FragmentsImmunoglobulin Variable RegionKineticsProtein BindingProtein Structure, TertiaryRecombinant ProteinsTumor Necrosis Factor-alphaDNA, ComplementaryImmunoglobulin FragmentsImmunoglobulin Variable RegionPeptide LibraryRecombinant ProteinsTumor Necrosis Factor-alpha

Identifiers

PMID12239343
PMCPMC130508

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.