Evidence map›Paper›PMID 22023457›Full record

ArticleMolecular microbiology2011

Either periplasmic tethering or protease resistance is sufficient to allow a SodC to protect Salmonella enterica serovar Typhimurium from phagocytic superoxide.

Marcus D Rushing, James M Slauch

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Characterization of Virulence Genotypes, Antimicrobial Resistance Patterns, and Biofilm Synthesis inThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2024
    Article
  2. Article
  3. Article
  4. Pathogens (Basel, Switzerland) · 2021
    Article
  5. Characterization ofAnimals : an open access journal from MDPI · 2020
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Mechanisms of copper homeostasis in bacteria.Frontiers in cellular and infection microbiology · 2013
    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.

Marcus D RushingDepartment of Microbiology, University of Illinois, Urbana, IL 61801, USA.
James M Slauch
University of Illinois Urbana-Champaign · US

Funding

Functional Analysis of Cu/Zn Superoxide DismutaseR01AI063230 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLAUCH, JAMES M. · 2005 to 2009
$1.7M
Regulation of the Salmonella Pathogenicity Island 1 Type III Secretion SystemR01AI080705 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI SLAUCH, JAMES M. · 2010 to 2013
$1.4M
Infection Biology Training GrantT32AI078876 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI SLAUCH, JAMES M. · 2010 to 2014
$892k
NIAID NIH HHS AI078876NIAID NIH HHS AI080705NIAID NIH HHS AI63230NIAID NIH HHS R01 AI063230NIAID NIH HHS R01 AI080705NIAID NIH HHS T32 AI078876
6 · The paper itself

Abstract

Salmonella Typhimurium combats phagocytic superoxide by producing the periplasmic superoxide dismutase, SodCI. The homologous protein, SodCII, is also produced during infection, but does not contribute to virulence. The proteins physically differ in that SodCI is dimeric, protease resistant and non-covalently tethered within the periplasm. Conversely, SodCII is a protease-sensitive monomer that is released normally from the periplasm by osmotic shock. To identify which properties correlate with virulence, we constructed over 20 enzymatically functional hybrid SodC proteins and assayed them for protease susceptibility, release by osmotic shock, multimerization and affinity for metal cofactors. Protease susceptibility maps to the C-terminus of SodCII, while SodCI residues 120-131 are required for tethering. A protease-resistant SodCII hybrid was able to substitute for SodCI during infection. Interestingly, a tethered but protease-sensitive SodCII hybrid was also able to confer protection. Thus, either tethering or protease resistance is sufficient for a SodC to function during infection. These results support our model that in the macrophage, the outer membrane of Salmonella is partially disrupted by antimicrobial peptides. Periplasmic proteins, including SodCII, are released and/or phagocytic proteases gain access. SodCI is both tethered within the periplasm and protease resistant, thereby surviving to detoxify superoxide.

Indexed as

Amino Acid SequenceMicrobial ViabilityMolecular Sequence DataOsmotic PressurePeriplasmPhagocytesProtein MultimerizationProteolysisRecombinant ProteinsSalmonella typhimuriumSequence Homology, Amino AcidSuperoxide DismutaseRecombinant ProteinsSuperoxide Dismutase

Identifiers

PMID22023457
PMCPMC3220996
OpenAlexW1479913570

What OpenQuestion holds

Textmetadata
LicenceTDM
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.