Evidence map›Paper›PMID 24950200›Full record

ArticlePloS one2014

A highly functional synthetic phage display library containing over 40 billion human antibody clones.

Marcel Weber, Emil Bujak, Alessia Putelli, Alessandra Villa, Mattia Matasci, Laura Gualandi, Teresa Hemmerle, Sarah Wulhfard, Dario Neri

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.6field-weighted citation impact, top 6% of its field
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

30 citing papers in PubMed, 51 citations in OpenAlex.

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  9. Selection of a PD-1 blocking antibody from a novel fully human phage display library.Protein science : a publication of the Protein Society · 2022
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  12. Frontiers in microbiology · 2022
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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

9 authors at 2 institutions in 1 country.

Marcel WeberDepartment of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences, ETH Zürich, Zürich, Switzerland; Philochem AG, Otelfingen, Switzerland.
Emil BujakDepartment of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences, ETH Zürich, Zürich, Switzerland; Philochem AG, Otelfingen, Switzerland.
Alessia PutelliDepartment of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences, ETH Zürich, Zürich, Switzerland; Philochem AG, Otelfingen, Switzerland.
Alessandra VillaPhilochem AG, Otelfingen, Switzerland.
Mattia MatasciPhilochem AG, Otelfingen, Switzerland.
Laura GualandiPhilochem AG, Otelfingen, Switzerland.
Teresa HemmerlePhilochem AG, Otelfingen, Switzerland.
Sarah WulhfardPhilochem AG, Otelfingen, Switzerland.
Dario NeriDepartment of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences, ETH Zürich, Zürich, Switzerland.
Philochem (Switzerland) · CHETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several synthetic antibody phage display libraries have been created and used for the isolation of human monoclonal antibodies. The performance of antibody libraries, which is usually measured in terms of their ability to yield high-affinity binding specificities against target proteins of interest, depends both on technical aspects (such as library size and quality of cloning) and on design features (which influence the percentage of functional clones in the library and their ability to be used for practical applications). Here, we describe the design, construction and characterization of a combinatorial phage display library, comprising over 40 billion human antibody clones in single-chain fragment variable (scFv) format. The library was designed with the aim to obtain highly stable antibody clones, which can be affinity-purified on protein A supports, even when used in scFv format. The library was found to be highly functional, as >90% of randomly selected clones expressed the corresponding antibody. When selected against more than 15 antigens from various sources, the library always yielded specific and potent binders, at a higher frequency compared to previous antibody libraries. To demonstrate library performance in practical biomedical research projects, we isolated the human antibody G5, which reacts both against human and murine forms of the alternatively spliced BCD segment of tenascin-C, an extracellular matrix component frequently over-expressed in cancer and in chronic inflammation. The new library represents a useful source of binding specificities, both for academic research and for the development of antibody-based therapeutics.

Indexed as

Peptide LibraryAnimalsAntibodies, MonoclonalAntibody SpecificityCloning, MolecularHumansMiceModels, MolecularProtein Structure, TertiaryTenascinAntibodies, MonoclonalPeptide LibraryTenascin

Identifiers

PMID24950200
PMCPMC4065035
OpenAlexW1965140525

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

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.