Evidence map›Paper›PMID 28272507›Full record

ArticleScientific reports2017

Scrutiny of Mycobacterium tuberculosis 19 kDa antigen proteoforms provides new insights in the lipoglycoprotein biogenesis paradigm.

Julien Parra, Julien Marcoux, Isabelle Poncin, Stéphane Canaan, Jean Louis Herrmann, Jérôme Nigou, Odile Burlet-Schiltz, Michel Rivière

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Methods for Proteomic Analyses of Mycobacteria.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  9. Targeted Lipidomics of Mycobacterial Lipids and Glycolipids.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  10. Evolution of Drug-ResistantFrontiers in microbiology · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Top-Down Proteomics: Ready for Prime Time?Analytical chemistry · 2018
    Review
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.

Julien ParraInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, France.
Julien MarcouxInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, France.
Isabelle PoncinAix Marseille Univ, CNRS, EIPL, IMM FR3479, Marseille, France.
Stéphane CanaanAix Marseille Univ, CNRS, EIPL, IMM FR3479, Marseille, France.
Jean Louis HerrmannUMR1173, INSERM, Université de Versailles St Quentin, 78180, Montigny le Bretonneux, France.
Jérôme NigouInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, France.
Odile Burlet-SchiltzInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, France.
Michel RivièreInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications (PTMs) are essential processes conditioning the biophysical properties and biological activities of the vast majority of mature proteins. However, occurrence of several distinct PTMs on a same protein dramatically increases its molecular diversity. The comprehensive understanding of the functionalities resulting from any particular PTM association requires a highly challenging full structural description of the PTM combinations. Here, we report the in-depth exploration of the natural structural diversity of the M. tuberculosis (Mtb) virulence associated 19 kDa lipoglycoprotein antigen (LpqH) using intact protein high-resolution mass spectrometry (HR-MS) coupled to liquid chromatography. Combined top-down and bottom-up HR-MS analyses of the purified Mtb LpqH protein allow, for the first time, to uncover a complex repertoire of about 130 molecular species resulting from the intrinsically heterogeneous combination of lipidation and glycosylation together with some truncations. Direct view on the co-occurring PTMs stoichiometry reveals the presence of functionally distinct LpqH lipidation states and indicates that glycosylation is independent from lipidation. This work allowed the identification of a novel unsuspected phosphorylated form of the unprocessed preprolipoglycoprotein totally absent from the current lipoglycoprotein biogenesis pathway and providing new insights into the biogenesis and functional determinants of the mycobacterial lipoglycoprotein interacting with the host immune PRRs.

Indexed as

ProteomeProteomicsAcetylationAmino Acid SequenceBacterial ProteinsChromatography, LiquidGlycoproteinsLipoproteinsModels, BiologicalMycobacterium tuberculosisPhosphorylationProtein Processing, Post-TranslationalTandem Mass Spectrometry19 kDa antigen, MycobacteriumBacterial ProteinsGlycoproteinsLipoproteinsProteome

Identifiers

PMID28272507
PMCPMC5341126

What OpenQuestion holds

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Registered trials

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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.