Evidence map›Paper›PMID 35194033›Full record

ArticleScientific reports2022

Proteome analysis of the Gram-positive fish pathogen Renibacterium salmoninarum reveals putative role of membrane vesicles in virulence.

Tobias Kroniger, Daniel Flender, Rabea Schlüter, Bernd Köllner, Anke Trautwein-Schult, Dörte Becher

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 34% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Immunomodulatory properties ofFrontiers in immunology · 2024
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  3. Dual RNA-Seq ofPathogens (Basel, Switzerland) · 2023
    Article
  4. Article
  5. Review
  6. 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

6 authors at 2 institutions in 1 country.

Tobias KronigerInstitute of Microbiology, Department of Microbial Proteomics, Center for Functional Genomics of Microbes, University of Greifswald, 17489, Greifswald, Germany.
Daniel FlenderInstitute of Microbiology, Department of Microbial Proteomics, Center for Functional Genomics of Microbes, University of Greifswald, 17489, Greifswald, Germany.
Rabea SchlüterImaging Center of the Department of Biology, University of Greifswald, 17489, Greifswald, Germany.
Bernd KöllnerInstitute of Immunology, Friedrich-Loeffler-Institute, Federal Research Institute for Animal Health, 17493, Greifswald - Isle of Riems, Germany.
Anke Trautwein-SchultInstitute of Microbiology, Department of Microbial Proteomics, Center for Functional Genomics of Microbes, University of Greifswald, 17489, Greifswald, Germany.
Dörte BecherInstitute of Microbiology, Department of Microbial Proteomics, Center for Functional Genomics of Microbes, University of Greifswald, 17489, Greifswald, Germany. dbecher@uni-greifswald.de.
Universität Greifswald · DEFriedrich-Loeffler-Institut · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial kidney disease (BKD) is a chronic bacterial disease affecting both wild and farmed salmonids. The causative agent for BKD is the Gram-positive fish pathogen Renibacterium salmoninarum. As treatment and prevention of BKD have proven to be difficult, it is important to know and identify the key bacterial proteins that interact with the host. We used subcellular fractionation to report semi-quantitative data for the cytosolic, membrane, extracellular, and membrane vesicle (MV) proteome of R. salmoninarum. These data can aid as a backbone for more targeted experiments regarding the development of new drugs for the treatment of BKD. Further analysis was focused on the MV proteome, where both major immunosuppressive proteins P57/Msa and P22 and proteins involved in bacterial adhesion were found in high abundance. Interestingly, the P22 protein was relatively enriched only in the extracellular and MV fraction, implicating that MVs may play a role in host-pathogen interaction. Compared to the other subcellular fractions, the MVs were also relatively enriched in lipoproteins and all four cell wall hydrolases belonging to the New Lipoprotein C/Protein of 60 kDa (NlpC/P60) family were detected, suggesting an involvement in the formation of the MVs.

Indexed as

ProteomicsVirulenceAnimalsBacterial AdhesionBacterial ProteinsCytoplasmic VesiclesFish DiseasesFishesHost-Parasite InteractionsKidney DiseasesLipoproteinsProteomeRenibacteriumSubcellular FractionsBacterial ProteinsLipoproteinsProteome

Identifiers

PMID35194033
PMCPMC8863785
OpenAlexW4212776248

What OpenQuestion holds

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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.