Evidence map›Paper›PMID 23216863›Full record

ArticleMolecular microbiology2013

Random mutagenesis and topology analysis of the autoinducing peptide biosynthesis proteins in Staphylococcus aureus.

Matthew Thoendel, Alexander R Horswill

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Determinants of maturation of theJournal of bacteriology · 2024
    Article
  3. Review
  4. Review
  5. Chemical and biomolecular insights into theIsrael journal of chemistry · 2023
    Article
  6. Article
  7. Review
  8. Review
  9. Interspecies Regulation BetweenFrontiers in microbiology · 2022
    Article
  10. Article
  11. Pathogenic Effect ofFrontiers in microbiology · 2020
    Article
  12. Article
  13. Regulation ofMicrobiology spectrum · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. The SaeRS Two-Component System Controls Survival ofFrontiers in cellular and infection microbiology · 2017
    Article
  19. Review
  20. Key driving forces in the biosynthesis of autoinducing peptides required for staphylococcal virulence.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

2 authors at 1 institution in 1 country.

Matthew ThoendelDepartment of Microbiology, Roy J and Lucille A Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.
Alexander R Horswill
University of Iowa · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007337 · NIGMS · UNIVERSITY OF IOWA · PI GEYER, PAMELA K., LENTZ, STEVEN R · 1985 to 2020
$15.9M
TRAINING IN MECHANISMS OF PARASITISMT32AI007511 · NIAID · UNIVERSITY OF IOWA · PI BUTLER, NOAH SULLIVAN, WEBER, MARY · 1996 to 2025
$8.1M
Quorum sensing-dependent interactions with biofilms and innate immunity defensesR01AI078921 · NIAID · UNIVERSITY OF IOWA · PI HORSWILL, ALEXANDER R · 2008 to 2012
$2.0M
NIAID NIH HHS AI078921NIAID NIH HHS R01 AI078921NIAID NIH HHS T32 AI007511NIAID NIH HHS T32 AI07511NIGMS NIH HHS T32 GM007337
6 · The paper itself

Abstract

The Staphylococcus aureus accessory gene regulator (agr) is a peptide signalling system that regulates the production of secreted virulence factors required to cause infections. The signal controlling agr function is a 7-9 residue thiolactone-containing peptide called an autoinducing peptide (AIP) that is biosynthesized from the AgrD precursor by the membrane peptidase AgrB. To gain insight into AgrB and AgrD function, the agrBD genes were mutagenized and screened for deficiencies in AIP production. In total, single-site mutations at 14 different residues in AgrD were identified and another 20 within AgrB. In AgrD, novel mutations were characterized in the N-terminal leader and throughout the central region encoding the AIP signal. In AgrB, most mutations blocked peptidase activity, but mutations in the K129-K131 residues were defective in a later step in AIP biosynthesis, separating the peptidase function from thiolactone ring formation and AIP transport. With the identification of residues in AgrB essential for AgrD processing, we reevaluated the membrane topology and the new model predicts four transmembrane helices and a potential re-entrant loop on the cytoplasmic face. Finally, co-immunoprecipitation studies indicate that AgrB forms oligomeric structures within the membrane. These studies provide further insight into the unique structural and functional properties of AgrB.

Indexed as

MutagenesisBacterial ProteinsCell MembraneDNA Mutational AnalysisModels, MolecularPeptides, CyclicStaphylococcus aureusAgrB protein, Staphylococcus aureusAgrD protein, StaphylococcusBacterial ProteinsPeptides, Cyclic

Identifiers

PMID23216863
PMCPMC3545067
OpenAlexW2131520604

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.