Evidence map›Paper›PMID 31601981›Full record

ArticleScientific reports2019

Mycoplasma hyopneumoniae surface-associated proteases cleave bradykinin, substance P, neurokinin A and neuropeptide Y.

Veronica Maria Jarocki, Benjamin Bernard Armando Raymond, Jessica Leigh Tacchi, Matthew Paul Padula, Steven Philip Djordjevic

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2019. 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
1.4field-weighted citation impact, top 21% 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, 17 citations in OpenAlex.

  1. Review
  2. RNA sequencing ofJournal of veterinary science · 2025
    Article
  3. Article
  4. Updated Methods for Elucidating Bacterial Surfaceomes.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  5. Review
  6. Hypothetical Proteins ofMicroorganisms · 2023
    Article
  7. Article
  8. Article
  9. TheFrontiers in microbiology · 2022
    Review
  10. The genome and antigen proteome analysis ofFrontiers in microbiology · 2022
    Article
  11. Review
  12. Review
  13. 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

5 authors at 1 institution in 1 country.

Veronica Maria Jarockiithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia. veronica.jarocki@uts.edu.au.
Benjamin Bernard Armando Raymondithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.
Jessica Leigh Tacchiithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.
Matthew Paul PadulaProteomics Core Facility, University of Technology Sydney, PO Box 123, Broadway, 2007, NSW, Australia.
Steven Philip Djordjevicithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia. steven.djordjevic@uts.edu.au.
University of Technology Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycoplasma hyopneumoniae is an economically-devastating and geographically-widespread pathogen that colonises ciliated epithelium, and destroys mucociliary function. M. hyopneumoniae devotes ~5% of its reduced genome to encode members of the P97 and P102 adhesin families that are critical for colonising epithelial cilia, but mechanisms to impair mucociliary clearance and manipulate host immune response to induce a chronic infectious state have remained elusive. Here we identified two surface exposed M. hyopneumoniae proteases, a putative Xaa-Pro aminopeptidase (MHJ_0659; PepP) and a putative oligoendopeptidase F (MHJ_0522; PepF), using immunofluorescence microscopy and two orthogonal proteomic methodologies. MHJ_0659 and MHJ_0522 were purified as polyhistidine fusion proteins and shown, using a novel MALDI-TOF MS assay, to degrade four pro-inflammatory peptides that regulate lung homeostasis; bradykinin (BK), substance P (SP), neurokinin A (NKA) and neuropeptide Y (NPY). These findings provide insight into the mechanisms used by M. hyopneumoniae to influence ciliary beat frequency, impair mucociliary clearance, and initiate a chronic infectious disease state in swine, features that are a hallmark of disease caused by this pathogen.

Indexed as

Adhesins, BacterialAminopeptidasesAnimalsBacterial ProteinsBradykininImmunity, InnateMetalloendopeptidasesMycoplasma hyopneumoniaeNeurokinin ANeuropeptide YProteomicsSubstance PSwineTrypsinAdhesins, BacterialAminopeptidasesBacterial ProteinsBradykininMetalloendopeptidasesNeurokinin ANeuropeptide YOligoendopeptidase FSubstance PTrypsin

Identifiers

PMID31601981
PMCPMC6787215
OpenAlexW2980145033

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.