Evidence map›Paper›PMID 27400835›Full record

ArticleProteomics. Clinical applications2016

A standardized production pipeline for high profile targets from Mycobacterium tuberculosis.

Morlin C Milewski, Tobias Broger, Joanna Kirkpatrick, Angela Filomena, Dana Komadina, Nicole Schneiderhan-Marra, Matthias Wilmanns, Annabel H A Parret

Open access · hybridAbstract read
In one paragraph

Article in Proteomics. Clinical applications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Differential levels of anti-Frontiers in medicine · 2023
    Article
  3. Article
  4. Article
  5. Diagnostic Performance of Tuberculosis-Specific IgG Antibody Profiles in Patients with Presumptive Tuberculosis from Two Continents.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2017
    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 4 institutions in 2 countries.

Morlin C MilewskiEuropean Molecular Biology Laboratory (EMBL), Hamburg Unit, Hamburg, Germany.
Tobias BrogerFoundation for Innovative New Diagnostics (FIND), Geneva, Switzerland.
Joanna KirkpatrickEuropean Molecular Biology Laboratory (EMBL), Proteomics Core Facility, Heidelberg, Germany.
Angela FilomenaNatural and Medical Sciences Institute, University of Tübingen, Reutlingen, Germany.
Dana KomadinaEuropean Molecular Biology Laboratory (EMBL), Hamburg Unit, Hamburg, Germany.
Nicole Schneiderhan-MarraNatural and Medical Sciences Institute, University of Tübingen, Reutlingen, Germany.
Matthias WilmannsEuropean Molecular Biology Laboratory (EMBL), Hamburg Unit, Hamburg, Germany.
Annabel H A ParretEuropean Molecular Biology Laboratory (EMBL), Hamburg Unit, Hamburg, Germany. parret@embl-hamburg.de.
European Molecular Biology Laboratory · DENatural and Medical Sciences Institute · DEFoundation for Innovative New Diagnostics · CHUniversity Medical Center Hamburg-Eppendorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeTuberculosis is still a major threat to global health. New tools and strategies to produce disease-related proteins are quintessential for the development of novel vaccines and diagnostic markers. EXPERIMENTAL

designTo obtain recombinant proteins from Mycobacterium tuberculosis (Mtb) for use in clinical applications, a standardized procedure was developed that includes subcloning, protein expression in Mycobacterium smegmatis and protein purification using chromatography. The potential for the different protein targets to serve as diagnostic markers for tuberculosis was established using multiplex immunoassays.

resultsTwelve soluble proteins from Mtb, including one protein complex, were purified to near-homogeneity following recombinant expression in M. smegmatis. Protein purity was assessed both by size exclusion chromatography and MS. Multiplex serological testing of the final protein preparations showed that all but one protein displayed a clear antibody response in serum samples from 278 tuberculosis patients. CONCLUSION AND CLINICAL RELEVANCE: The established workflow comprises a simple, cost-effective, and scalable pipeline for production of soluble proteins from Mtb and can be used to prioritize immunogenic proteins suitable for use as diagnostic markers.

Indexed as

Antibodies, BacterialBacterial ProteinsCloning, MolecularGene Expression Regulation, BacterialHumansMass SpectrometryMycobacterium tuberculosisProteomicsReference StandardsSolubilityTuberculosisAntibodies, BacterialBacterial ProteinsAntigenMultiplex immunoassayMycobacteriumRecombinant protein production

Identifiers

PMID27400835
PMCPMC5095800
OpenAlexW2469103144

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.