Evidence map›Paper›PMID 24928312›Full record

ArticleMicrobiology (Reading, England)2014

The lone S41 family C-terminal processing protease in Staphylococcus aureus is localized to the cell wall and contributes to virulence.

Ronan K Carroll, Frances E Rivera, Courtney K Cavaco, Grant M Johnson, David Martin, Lindsey N Shaw

Open access · greenAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2014. 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
0.5field-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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Tail-specific protease is an essentialInfection and immunity · 2024
    Article
  2. Article
  3. Review
  4. The identification of two M20B family peptidases required for full virulence inFrontiers in cellular and infection microbiology · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Frontiers in genetics · 2021
    Article
  13. Mutation of the Carboxy-Terminal Processing Protease inPathogens (Basel, Switzerland) · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 1 institution in 1 country.

Ronan K CarrollDepartment of Cell Biology, Microbiology & Molecular Biology, University of South Florida, Tampa, FL, USA.
Frances E RiveraDepartment of Cell Biology, Microbiology & Molecular Biology, University of South Florida, Tampa, FL, USA.
Courtney K CavacoDepartment of Cell Biology, Microbiology & Molecular Biology, University of South Florida, Tampa, FL, USA.
Grant M JohnsonDepartment of Cell Biology, Microbiology & Molecular Biology, University of South Florida, Tampa, FL, USA.
David MartinDepartment of Cell Biology, Microbiology & Molecular Biology, University of South Florida, Tampa, FL, USA.
Lindsey N ShawDepartment of Cell Biology, Microbiology & Molecular Biology, University of South Florida, Tampa, FL, USA.
University of South Florida · US

Funding

Characterization of ??S in the stress & virulence responses of S. aureusR01AI080626 · NIAID · UNIVERSITY OF SOUTH FLORIDA · PI SHAW, LINDSEY NEIL · 2010 to 2013
$1.3M
Exploring the Influence of an Intracellular Aminopeptidase on S. aureus VirulenceR21AI109389 · NIAID · UNIVERSITY OF SOUTH FLORIDA · PI SHAW, LINDSEY NEIL · 2014 to 2015
$402k
NIAID NIH HHS AI080626NIAID NIH HHS AI109389NIAID NIH HHS R01 AI080626NIAID NIH HHS R21 AI109389
6 · The paper itself

Abstract

Staphylococcus aureus is a versatile pathogen of humans and a continued public health concern due to the rise and spread of multidrug-resistant strains. As part of an ongoing investigation into the pathogenic mechanisms of this organism we previously demonstrated that an intracellular N-terminal processing protease is required for S. aureus virulence. Following on from this, here we examine the role of CtpA, the lone C-terminal processing protease of S. aureus. CtpA, a member of the S41 family, is a serine protease whose homologues in Gram-negative bacteria have been implicated in a range of biological functions, including pathogenesis. We demonstrate that S. aureus CtpA is localized to the bacterial cell wall and expression of the ctpA gene is maximal upon exposure to conditions encountered during infection. Disruption of the ctpA gene leads to decreased heat tolerance and increased sensitivity when exposed to components of the host immune system. Finally we demonstrate that the ctpA(-) mutant strain is attenuated for virulence in a murine model of infection. Our results represent the first characterization of a C-terminal processing protease in a pathogenic Gram-positive bacterium and show that it plays a critical role during infection.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsCell WallEndopeptidasesGene Expression Regulation, BacterialHumansMiceMolecular Sequence DataMultigene FamilyProtein TransportSequence AlignmentStaphylococcal InfectionsStaphylococcus aureusVirulenceBacterial ProteinsC-terminal processing peptidaseEndopeptidases

Identifiers

PMID24928312
PMCPMC4117222
OpenAlexW2020573494

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.