Evidence map›Paper›PMID 25589579›Full record

ArticleOpen biology2015

MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae.

Veronica M Jarocki, Jerran Santos, Jessica L Tacchi, Benjamin B A Raymond, Ania T Deutscher, Cheryl Jenkins, Matthew P Padula, Steven P Djordjevic

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

Article in Open biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.6field-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

35 citing papers in PubMed, 63 citations in OpenAlex.

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  9. TheFrontiers in microbiology · 2022
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  15. Review
  16. Combined Transcriptome Sequencing ofFrontiers in microbiology · 2020
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  17. Article
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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

8 authors at 2 institutions in 1 country.

Veronica M JarockiThe ithree institute, University of Technology, Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
Jerran SantosThe 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.
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.
Ania T DeutscherNSW Department of Primary Industries, Private Bag 4008, Narellan, New South Wales 2567, Australia.
Cheryl JenkinsNSW Department of Primary Industries, Private Bag 4008, Narellan, New South Wales 2567, Australia.
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 · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminopeptidases are part of the arsenal of virulence factors produced by bacterial pathogens that inactivate host immune peptides. Mycoplasma hyopneumoniae is a genome-reduced pathogen of swine that lacks the genetic repertoire to synthesize amino acids and relies on the host for availability of amino acids for growth. M. hyopneumoniae recruits plasmin(ogen) onto its cell surface via the P97 and P102 adhesins and the glutamyl aminopeptidase MHJ_0125. Plasmin plays an important role in regulating the inflammatory response in the lungs of pigs infected with M. hyopneumoniae. We show that recombinant MHJ_0461 (rMHJ_0461) functions as a leucine aminopeptidase (LAP) with broad substrate specificity for leucine, alanine, phenylalanine, methionine and arginine and that MHJ_0461 resides on the surface of M. hyopneumoniae. rMHJ_0461 also binds heparin, plasminogen and foreign DNA. Plasminogen bound to rMHJ_0461 was readily converted to plasmin in the presence of tPA. Computational modelling identified putative DNA and heparin-binding motifs on solvent-exposed sites around a large pore on the LAP hexamer. We conclude that MHJ_0461 is a LAP that moonlights as a multifunctional adhesin on the cell surface of M. hyopneumoniae.

Indexed as

Amino AcidsAmino Acid SequenceBacterial ProteinsBinding SitesHeparinLeucyl AminopeptidaseMembrane ProteinsMolecular Sequence DataMycoplasma hyopneumoniaePlasminogenProtein BindingSubstrate SpecificityAmino AcidsBacterial ProteinsHeparinLeucyl AminopeptidaseMembrane ProteinsPlasminogenadhesinDNA-binding proteinheparin-binding proteinleucine aminopeptidasemoonlighting proteinplasminogen-binding protein

Identifiers

PMID25589579
PMCPMC4313372
OpenAlexW1985097161

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.