Evidence map›Paper›PMID 12936988›Full record

ArticleAntimicrobial agents and chemotherapy2003

Intracellular expression of Peptide fusions for demonstration of protein essentiality in bacteria.

R Edward Benson, Elizabeth B Gottlin, Dale J Christensen, Paul T Hamilton

Open access · greenAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Structure, inhibition, and regulation of essential lipid A enzymes.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  6. Lipid A as a Drug Target and Therapeutic Molecule.Biomolecules & therapeutics · 2015
    Review
  7. Article
  8. TetR-based gene regulation systems for Francisella tularensis.Applied and environmental microbiology · 2012
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  14. Article
  15. Structure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptide.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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 at 1 institution in 1 country.

R Edward BensonKaro Bio USA, Inc, Durham, NC 27703, USA.
Elizabeth B Gottlin
Dale J Christensen
Paul T Hamilton
Karo Pharma (Sweden) · SE

Funding

A NOVEL APPROACH TO THE DISCOVERY OF ANTIBACTERIAL DRUGSR43AI046036 · NIAID · NOVALON PHARMACEUTICAL CORPORATION · PI HAMILTON, PAUL T · 1999 to 2000
$102k
NIAID NIH HHS 5R43 AI46036-02
6 · The paper itself

Abstract

We describe a "protein knockout" technique that can be used to identify essential proteins in bacteria. This technique uses phage display to select peptides that bind specifically to purified target proteins. The peptides are expressed intracellularly and cause inhibition of growth when the protein is essential. In this study, peptides that each specifically bind to one of seven essential proteins were identified by phage display and then expressed as fusions to glutathione S-transferase in Escherichia coli. Expression of peptide fusions directed against E. coli DnaN, LpxA, RpoD, ProRS, SecA, GyrA, and Era each dramatically inhibited cell growth. Under the same conditions, a fusion with a randomized peptide sequence did not inhibit cell growth. In growth-inhibited cells, inhibition could be relieved by concurrent overexpression of the relevant target protein but not by coexpression of an irrelevant protein, indicating that growth inhibition was due to a specific interaction of the expressed peptide with its target. The protein knockout technique can be used to assess the essentiality of genes of unknown function emerging from the sequencing of microbial genomes. This technique can also be used to validate proteins as drug targets, and their corresponding peptides as screening tools, for discovery of new antimicrobial agents.

Indexed as

Bacterial ProteinsBlotting, WesternCulture MediaDNA, BacterialDNA ReplicationDNA, SuperhelicalEscherichia coliGenetic VectorsPeptide LibraryPeptidesPlasmidsProtein BiosynthesisReverse Transcriptase Polymerase Chain ReactionTranscription, GeneticBacterial ProteinsCulture MediaDNA, BacterialDNA, SuperhelicalPeptide LibraryPeptides

Identifiers

PMID12936988
PMCPMC182649
OpenAlexW2112849014

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.