Evidence map›Paper›PMID 36744901›Full record

ArticlemBio2023

Contribution of Extracellular Membrane Vesicles To the Secretome of Staphylococcus aureus.

Divakara Ssm Uppu, Xiaogang Wang, Jean C Lee

Open access · goldAbstract read
In one paragraph

Article in mBio, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  6. Proteolytically activated antibacterial toxins inhibit the growth of diverse gram-positive bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  7. Review
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  9. Review
  10. Linking Virulence and Iron Limitation Response inJournal of proteome research · 2025
    Article
  11. Integrated genomic and proteomic analysis of the mouse-adaptedCurrent research in microbial sciences · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. 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

3 authors at 1 institution in 1 country.

Divakara Ssm UppuDivision of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, USA.
Xiaogang WangDivision of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, USA.
Jean C LeeDivision of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, USA.ORCID 0000-0002-8094-5180
Brigham and Women's Hospital · US

Funding

Staphylococcus aureus extracellular vesicles: host-pathogen interactionsR01AI141885 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI WANG, XIAOGANG · 2019 to 2022
$2.1M
NIAID NIH HHS R01 AI141885
6 · The paper itself

Abstract

The microbial secretome modulates how the organism interacts with its environment. Included in the Staphylococcus aureus secretome are extracellular membrane vesicles (MVs) that consist of cytoplasmic and membrane proteins, as well as exoproteins, some cell wall-associated proteins, and glycopolymers. The extent to which MVs contribute to the diverse composition of the secretome is not understood. We performed a proteomic analysis of MVs purified from the S. aureus strain MRSA252 along with a similar analysis of the whole secretome (culture supernatant) before and after depletion of MVs. The MRSA252 secretome was comprised of 1,001 proteins, of which 667 were also present in MVs. Cell membrane-associated proteins and lipoteichoic acid in the culture supernatant were highly associated with MVs, followed by cytoplasmic and extracellular proteins. Few cell wall-associated proteins were contained in MVs, and capsular polysaccharides were found both in the secretome and MVs. When MVs were removed from the culture supernatant by ultracentrifugation, 54 of the secretome proteins were significantly depleted in abundance. Proteins packaged in MVs were characterized by an isoelectric point that was significantly higher than that of proteins excluded from MVs. Our data indicate that the generation of S. aureus MVs is a mechanism by which lipoteichoic acid, cytoplasmic, and cell membrane-associated proteins are released into the secretome.

Indexed as

Extracellular VesiclesStaphylococcal InfectionsHumansMembrane ProteinsProteomicsSecretomeStaphylococcus aureusMembrane Proteinsextracellular membrane vesiclemembrane proteinsproteomicssecretomeStaphylococcus aureus

Identifiers

PMID36744901
PMCPMC9973311
OpenAlexW4319294027

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.