Evidence map›Paper›PMID 11861923›Full record

ArticleNucleic acids research2002

An improved helper phage system for efficient isolation of specific antibody molecules in phage display.

Hyunjung Baek, Kyoung-ho Suk, Yong-hwan Kim, Sanghoon Cha

Abstract read
In one paragraph

Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Progress in phage display: evolution of the technique and its application.Cellular and molecular life sciences : CMLS · 2010
    Review
  17. Article
  18. Article
  19. Eliminating helper phage from phage display.Nucleic acids research · 2006
    Article
  20. Toward cocaine esterase therapeutics.Journal of the American Chemical Society · 2005
    Article
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

4 authors.

Hyunjung BaekIG Therapy Co., Nong 3rd Building 112, Kangwon National University, Chunchon 200-701, South Korea.
Kyoung-ho Suk
Yong-hwan Kim
Sanghoon Cha

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phage display technology has been applied in many fields of biological and medical sciences to study molecular interactions and especially in the generation of monoclonal antibodies of human origin. However, extremely low display level of antibody molecules on the surface of phage is an intrinsic problem of a phagemid-based display system resulting in low success rate of isolating specific binding molecules. We show here that display of single-chain antibody fragment (scFv) generated with pIGT3 phagemid can be increased dramatically by using a genetically modified Ex-phage. Ex-phage has a mutant pIII gene that produces a functional wild-type pIII in suppressing Escherichia coli strains but does not make any pIII in non-suppressing E.coli strains. Packaging phagemids encoding antibody-pIII fusion in F+ non-suppressing E.coli strains with Ex-phage enhanced the display level of antibody fragments on the surfaces of recombinant phage particles resulting in an increase of antigen-binding reactivity >100-fold compared to packaging with M13KO7 helper phage. Thus, the Ex-phage and pIGT3 phagemid vector provides a system for the efficient enrichment of specific binding antibodies from a phage display library and, thereby, increases the chance of obtaining more diverse antibodies specific for target antigens.

Indexed as

Peptide LibraryAmino Acid SequenceAntibodiesAntibody SpecificityBacteriophage M13Base SequenceCapsid ProteinsDNA-Binding ProteinsEnzyme-Linked Immunosorbent AssayEscherichia coliGenetic VectorsHSP70 Heat-Shock ProteinsImmunoblottingImmunoglobulin FragmentsMolecular Sequence DataMutagenesis, Site-DirectedAntibodiesCapsid ProteinsDNA-Binding ProteinsHSP70 Heat-Shock ProteinsImmunoglobulin FragmentsPeptide LibraryRecombinant Fusion ProteinsViral Fusion Proteins

Identifiers

PMID11861923
PMCPMC101254

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.