Evidence map›Paper›PMID 22447899›Full record

ArticleJournal of bacteriology2012

Type I signal peptidase and protein secretion in Staphylococcus aureus.

Mark A Schallenberger, Sherry Niessen, Changxia Shao, Bruce J Fowler, Floyd E Romesberg

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

41 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
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  7. Article
  8. Article
  9. Review
  10. GFP fusions of Sec-routed extracellular proteins inMicrobial cell (Graz, Austria) · 2023
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  12. Proteomic Comparison of Ivermectin Sensitive and ResistantAntibiotics (Basel, Switzerland) · 2022
    Article
  13. Article
  14. Article
  15. Crystal Structure of CytochromeJournal of microbiology and biotechnology · 2020
    Article
  16. Article
  17. Structural basis for theThe Journal of biological chemistry · 2020
    Article
  18. Article
  19. Article
  20. Inhibition of Protein Secretion inAntimicrobial agents and chemotherapy · 2019
    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

5 authors at 1 institution in 1 country.

Mark A SchallenbergerDepartment of Chemistry, The Scripps Research Institute, La Jolla, California, USA.
Sherry Niessen
Changxia Shao
Bruce J Fowler
Floyd E Romesberg
Scripps Research Institute · US

Funding

Re-engineering the arylomycins for antibiotic activityR21AI081126 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI ROMESBERG, FLOYD E. · 2009 to 2010
$495k
NIAID NIH HHS AI081126NIAID NIH HHS R21 AI081126
6 · The paper itself

Abstract

Staphylococcus aureus is an important human pathogen whose virulence relies on the secretion of many different proteins. In general, the secretion of most proteins in S. aureus, as well as other bacteria, is dependent on the type I signal peptidase (SPase)-mediated cleavage of the N-terminal signal peptide that targets a protein to the general secretory pathway. The arylomycins are a class of natural product antibiotics that inhibit SPase, suggesting that they may be useful chemical biology tools for characterizing the secretome. While wild-type S. aureus (NCTC 8325) is naturally resistant to the arylomycins, sensitivity is conferred via a point mutation in its SPase. Here, we use a synthetic arylomycin along with a sensitized strain of S. aureus and multidimensional protein identification technology (MudPIT) mass spectrometry to identify 46 proteins whose extracellular accumulation requires SPase activity. Forty-four possess identifiable Sec-type signal peptides and thus are likely canonically secreted proteins, while four also appear to possess cell wall retention signals. We also identified the soluble C-terminal domains of two transmembrane proteins, lipoteichoic acid synthase, LtaS, and O-acyteltransferase, OatA, both of which appear to have noncanonical, internal SPase cleavage sites. Lastly, we identified three proteins, HtrA, PrsA, and SAOUHSC_01761, whose secretion is induced by arylomycin treatment. In addition to elucidating fundamental aspects of the physiology and pathology of S. aureus, the data suggest that an arylomycin-based therapeutic would reduce virulence while simultaneously eradicating an infection.

Indexed as

Anti-Bacterial AgentsBacterial ProteinsGene Expression ProfilingGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicMembrane ProteinsOligopeptidesPeptides, CyclicPoint MutationProtein ConformationSerine EndopeptidasesStaphylococcus aureusVirulence FactorsAnti-Bacterial Agentsarylomycin A-C16Bacterial ProteinsMembrane ProteinsOligopeptidesPeptides, CyclicSerine Endopeptidasestype I signal peptidaseVirulence Factors

Identifiers

PMID22447899
PMCPMC3347181
OpenAlexW2093138731

What OpenQuestion holds

Textmetadata
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.