Evidence map›Paper›PMID 24459079›Full record

ArticleProteomics2014

Complete posttranslational modification mapping of pathogenic Neisseria meningitidis pilins requires top-down mass spectrometry.

Joseph Gault, Christian Malosse, Silke Machata, Corinne Millien, Isabelle Podglajen, Marie-Cécile Ploy, Catherine E Costello, Guillaume Duménil, Julia Chamot-Rooke

Open access · greenAbstract read
In one paragraph

Article in Proteomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
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  6. Protein-species quantitative venomics: looking through a crystal ball.The journal of venomous animals and toxins including tropical diseases · 2017
    Review
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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

9 authors at 7 institutions in 2 countries.

Joseph GaultStructural Mass Spectrometry and Proteomics Unit, Institut Pasteur, CNRS UMR 3528, Paris, France; Laboratoire des Mécanismes Réactionnels (DCMR), Département de Chimie, École Polytechnique, CNRS, Palaiseau, France.
Christian Malosse
Silke Machata
Corinne Millien
Isabelle Podglajen
Marie-Cécile Ploy
Catherine E Costello
Guillaume Duménil
Julia Chamot-Rooke
Centre National de la Recherche Scientifique · FRInserm · FRAssistance Publique – Hôpitaux de Paris · FRBoston University · USÉcole Polytechnique · FRUniversité de Limoges · FRUniversité Paris Cité · FR

Funding

XI INTERNATIONAL SYMPOSIUM ON AMYLOIDOSISP41RR010888 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 1996 to 2011
$18.6M
Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
LTQ-FT MS System for On-line Protein and Glycan AnalysisS10RR025082 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2009 to 2009
$1.3M
NCRR NIH HHS P41 RR010888NCRR NIH HHS S10 RR025082NHLBI NIH HHS HHSN268201000031CNIGMS NIH HHS P41 GM104603
6 · The paper itself

Abstract

In pathogenic bacteria, posttranslationally modified proteins have been found to promote bacterial survival, replication, and evasion from the host immune system. In the human pathogen Neisseria meningitidis, the protein PilE (15-18 kDa) is the major building block of type IV pili, extracellular filamentous organelles that play a major role in mediating pathogenesis. Previous reports have shown that PilE can be expressed as a number of different proteoforms, each harboring its own set of PTMs and that specific proteoforms are key in promoting bacterial virulence. Efficient tools that allow complete PTM mapping of proteins involved in bacterial infection are therefore strongly needed. As we show in this study, a simple combination of mass profiling and bottom-up proteomics is fundamentally unable to achieve this goal when more than two proteoforms are present simultaneously. In a N. meningitidis strain isolated from a patient with meningitis, mass profiling revealed the presence of four major proteoforms of PilE, in a 1:1:1:1 ratio. Due to the complexity of the sample, a top-down approach was required to achieve complete PTM mapping for all four proteoforms, highlighting an unprecedented extent of glycosylation. Top-down MS therefore appears to be a promising tool for the analysis of highly posttranslationally modified proteins involved in bacterial virulence.

Indexed as

Amino Acid SequenceFimbriae ProteinsMass SpectrometryMolecular Sequence DataNeisseria meningitidisPeptide FragmentsPeptide MappingProtein Processing, Post-TranslationalProteomicsFimbriae ProteinsPeptide FragmentsNeisseria meningitidisPiliProteoformsPTMTechnologyTop-down MS

Identifiers

PMID24459079
PMCPMC4201860
OpenAlexW2026095002

What OpenQuestion holds

Textmetadata
LicenceTDM
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.