Evidence map›Paper›PMID 28077594›Full record

ArticleOpen biology2017

The N-linking glycosylation system from Actinobacillus pleuropneumoniae is required for adhesion and has potential use in glycoengineering.

Jon Cuccui, Vanessa S Terra, Janine T Bossé, Andreas Naegeli, Sherif Abouelhadid, Yanwen Li, Chia-Wei Lin, Prerna Vohra, Alexander W Tucker, Andrew N Rycroft and 5 more

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2017. 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
2.5field-weighted citation impact, top 11% 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, 34 citations in OpenAlex.

  1. Rational design of a highly activeEngineering microbiology · 2024
    Article
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  4. Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020
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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

15 authors at 5 institutions in 2 countries.

Jon CuccuiFaculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK.ORCID 0000-0002-4538-4007
Vanessa S TerraFaculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK.ORCID 0000-0002-2734-4036
Janine T BosséSection of Paediatrics, Department of Medicine, Imperial College London, St. Mary's Campus, London W2 1PG, UK.
Andreas NaegeliInstitute of Microbiology, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zürich, Switzerland.ORCID 0000-0002-5938-9124
Sherif AbouelhadidFaculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK.
Yanwen LiSection of Paediatrics, Department of Medicine, Imperial College London, St. Mary's Campus, London W2 1PG, UK.
Chia-Wei LinInstitute of Microbiology, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zürich, Switzerland.
Prerna VohraFaculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK.
Alexander W TuckerDepartment of Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge CB3 0ES, UK.
Andrew N RycroftThe Royal Veterinary College, Hawkshead Campus, Hatfield, Hertfordshire AL9 7TA, UK.
Duncan J MaskellDepartment of Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge CB3 0ES, UK.
Markus AebiInstitute of Microbiology, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zürich, Switzerland.
Paul R LangfordSection of Paediatrics, Department of Medicine, Imperial College London, St. Mary's Campus, London W2 1PG, UK.
Brendan W WrenFaculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK brendan.wren@lshtm.ac.uk.ORCID 0000-0002-6140-9489
BRaDP1T Consortium
University of London · GBETH Zurich · CHSt Mary's Hospital · GBUniversity of Cambridge · GBRoyal Veterinary College · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G003203/1Biotechnology and Biological Sciences Research Council BB/G018553/1Biotechnology and Biological Sciences Research Council BB/G019177/1Biotechnology and Biological Sciences Research Council BB/G019274/1Biotechnology and Biological Sciences Research Council BB/G020744/1Biotechnology and Biological Sciences Research Council BBS/B/04862Biotechnology and Biological Sciences Research Council E20372Wellcome Trust 102979/Z/13/ZWellcome Trust 105609/Z/14/Z
6 · The paper itself

Abstract

Actinobacillus pleuropneumoniae is a mucosal respiratory pathogen causing contagious porcine pleuropneumonia. Pathogenesis studies have demonstrated a major role for the capsule, exotoxins and outer membrane proteins. Actinobacillus pleuropneumoniae can also glycosylate proteins, using a cytoplasmic N-linked glycosylating enzyme designated NGT, but its transcriptional arrangement and role in virulence remains unknown. We investigated the NGT locus and demonstrated that the putative transcriptional unit consists of rimO, ngt and a glycosyltransferase termed agt. From this information we used the A. pleuropneumoniae glycosylation locus to decorate an acceptor protein, within Escherichia coli, with a hexose polymer that reacted with an anti-dextran antibody. Mass spectrometry analysis of a truncated protein revealed that this operon could add up to 29 repeat units to the appropriate sequon. We demonstrated the importance of NGT in virulence, by creating deletion mutants and testing them in a novel respiratory cell line adhesion model. This study demonstrates the importance of the NGT glycosylation system for pathogenesis and its potential biotechnological application for glycoengineering.

Indexed as

OperonA549 CellsActinobacillus pleuropneumoniaeBacterial ProteinsCell AdhesionCloning, MolecularEscherichia coliGene Expression Regulation, BacterialGlycosylationHumansProtein EngineeringVirulence FactorsBacterial ProteinsVirulence FactorsActinobacillus pleuropneumoniaeadhesionN-linked glycosylation

Identifiers

PMID28077594
PMCPMC5303269
OpenAlexW2573883534

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.