Evidence map›Paper›PMID 24265677›Full record

ArticlePloS one2013

High-throughput sequencing enhanced phage display identifies peptides that bind mycobacteria.

Nqobile A C Ngubane, Lionel Gresh, Thomas R Ioerger, James C Sacchettini, Yanjia J Zhang, Eric J Rubin, Alexander Pym, Makobetsa Khati

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Next-Generation Phage Display to Identify Peptide Ligands of Deubiquitinases.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  3. Article
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  8. Biopanning data bank 2018: hugging next generation phage display.Database : the journal of biological databases and curation · 2018
    Article
  9. Article
  10. BDB: biopanning data bank.Nucleic acids research · 2016
    Article
  11. Article
  12. Article
  13. Article
  14. 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

8 authors at 6 institutions in 2 countries.

Nqobile A C NgubaneEmerging Health Technologies Platform, Council for Scientific and Industrial Research, Biosciences Unit, Pretoria, Gauteng, South Africa ; KwaZulu-Natal Research Institute for Tuberculosis and Human Immunodeficiency Virus, Nelson R. Mandela School of Medicine, University of KwaZulu-Natal, Durban, South Africa.
Lionel Gresh
Thomas R Ioerger
James C Sacchettini
Yanjia J Zhang
Eric J Rubin
Alexander Pym
Makobetsa Khati
Texas A&M University · USUniversity of KwaZulu-Natal · ZACouncil for Scientific and Industrial Research · ZAHarvard University · USMassachusetts Department of Public Health · USUniversity of Cape Town · ZA

Funding

Medical Scientist Training ProgramT32GM007753 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WALENSKY, LOREN DAVID · 1985 to 2021
$50.0M
IMMUNOLOGY AND INFECTIOUS DISEASES IN PUBLIC HEALTHT32AI007638 · NIAID · HARVARD UNIVERSITY (SCH OF PUBLIC HLTH) · PI RUBIN, ERIC J. · 2000 to 2014
$2.2M
NIAID NIH HHS T32 AI007638NIGMS NIH HHS T32 GM007753
6 · The paper itself

Abstract

Bacterial cell wall components have been previously used as infection biomarkers detectable by antibodies. However, it is possible that the surface of the Mycobacterium tuberculosis (M. tb), the causative agent of tuberculosis (TB), also possesses molecules which might be non-antigenic. This makes the probing of biomarkers on the surface of M. tb cell wall difficult using antibodies. Here we demonstrate the use of phage display technology to identify peptides that bind to mycobacteria. We identified these clones using both random clone picking and high throughput sequencing. We demonstrate that random clone picking does not necessarily identify highly enriched clones. We further showed that the clone displaying the CPLHARLPC peptide which was identified by Illumina sequencing as the most enriched, binds better to mycobacteria than three clones selected by random picking. Using surface plasmon resonance, we showed that chemically synthesised CPLHARLPC peptide binds to a 15 KDa peptide from M.tb H37Rv whole cell lysates. These observations demonstrate that phage display technology combined with high-throughput sequencing is a powerful tool to identify peptides that can be used for investigating potential non-antigenic biomarkers for TB and other bacterial infections.

Indexed as

High-Throughput Screening AssaysPeptide LibraryCell WallMycobacterium tuberculosisOligopeptidesProtein BindingOligopeptidesPeptide Library

Identifiers

PMID24265677
PMCPMC3827053
OpenAlexW2053315684

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.