Evidence map›Paper›PMID 26865024›Full record

ArticleOpen biology2016

Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae.

Jessica L Tacchi, Benjamin B A Raymond, Paul A Haynes, Iain J Berry, Michael Widjaja, Daniel R Bogema, Lauren K Woolley, Cheryl Jenkins, F Chris Minion, Matthew P Padula and 1 more

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
6.9field-weighted citation impact, top 3% 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

43 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Updated Methods for Elucidating Bacterial Surfaceomes.Methods in molecular biology (Clifton, N.J.) · 2025
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  4. Review
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  6. Genetic structure and diversity ofFrontiers in veterinary science · 2024
    Article
  7. A subunit vaccine based on P97R1, P46, P42, and P65 fromFrontiers in veterinary science · 2024
    Article
  8. Article
  9. Unveiling the stealthy tactics: mycoplasma's immune evasion strategies.Frontiers in cellular and infection microbiology · 2023
    Review
  10. Article
  11. Characterisation of thePathogens (Basel, Switzerland) · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. TheFrontiers in microbiology · 2022
    Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Mycoplasma bovisJournal of bacteriology · 2020
    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

11 authors at 4 institutions in 2 countries.

Jessica L TacchiThe ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
Benjamin B A RaymondThe ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
Paul A HaynesDepartment of Chemistry and Biomolecular Sciences, Macquarie University, North Ryde, New South Wales 2109, Australia.
Iain J BerryThe ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
Michael WidjajaThe ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
Daniel R BogemaThe ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia NSW Department of Primary Industries, Elizabeth Macarthur Agricultural Institute, Menangle, New South Wales 2568, Australia.
Lauren K WoolleyNSW Department of Primary Industries, Elizabeth Macarthur Agricultural Institute, Menangle, New South Wales 2568, Australia School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia.
Cheryl JenkinsNSW Department of Primary Industries, Elizabeth Macarthur Agricultural Institute, Menangle, New South Wales 2568, Australia.
F Chris MinionDepartment of Veterinary Microbiology and Preventative Medicine, Iowa State University, Ames, IA 50011, USA.
Matthew P PadulaThe ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia Proteomics Core Facility, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
Steven P DjordjevicThe ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia Proteomics Core Facility, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia steven.djordjevic@uts.edu.au.
University of Technology Sydney · AUNew South Wales Department of Primary Industries · AUIowa State University · USMacquarie University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycoplasma hyopneumoniae is a genome-reduced, cell wall-less, bacterial pathogen with a predicted coding capacity of less than 700 proteins and is one of the smallest self-replicating pathogens. The cell surface of M. hyopneumoniae is extensively modified by processing events that target the P97 and P102 adhesin families. Here, we present analyses of the proteome of M. hyopneumoniae-type strain J using protein-centric approaches (one- and two-dimensional GeLC-MS/MS) that enabled us to focus on global processing events in this species. While these approaches only identified 52% of the predicted proteome (347 proteins), our analyses identified 35 surface-associated proteins with widely divergent functions that were targets of unusual endoproteolytic processing events, including cell adhesins, lipoproteins and proteins with canonical functions in the cytosol that moonlight on the cell surface. Affinity chromatography assays that separately used heparin, fibronectin, actin and host epithelial cell surface proteins as bait recovered cleavage products derived from these processed proteins, suggesting these fragments interact directly with the bait proteins and display previously unrecognized adhesive functions. We hypothesize that protein processing is underestimated as a post-translational modification in genome-reduced bacteria and prokaryotes more broadly, and represents an important mechanism for creating cell surface protein diversity.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceBacterial ProteinsMembrane ProteinsMolecular Sequence DataMycoplasma hyopneumoniaeProteolysisProteomeProteomicsBacterial ProteinsMembrane ProteinsMycoplasma protein 65-kDaProteomeadhesinsglobal proteomeprocessingprotein-centrictwo-dimensional gels

Identifiers

PMID26865024
PMCPMC4772806
OpenAlexW2335623175

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.