Evidence map›Paper›PMID 16333395›Full record

ReviewPLoS pathogens2005

A novel endogenous inhibitor of the secreted streptococcal NAD-glycohydrolase.

Michael A Meehl, Jerome S Pinkner, Patricia J Anderson, Scott J Hultgren, Michael G Caparon

Open access · goldAbstract readReview
In one paragraph

Review in PLoS pathogens, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

39 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Immunomodulating Enzymes fromMicroorganisms · 2024
    Review
  4. Article
  5. Microorganisms · 2022
    Article
  6. Article
  7. Pathogen induced subversion of NADCell death discovery · 2021
    Article
  8. Group AAutophagy · 2020
    Article
  9. Article
  10. Article
  11. NADNature communications · 2018
    Article
  12. NAD-Glycohydrolase Depletes Intracellular NADFrontiers in microbiology · 2018
    Article
  13. Binding of NADmBio · 2017
    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

5 authors at 1 institution in 1 country.

Michael A MeehlDepartment of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri, USA.
Jerome S Pinkner
Patricia J Anderson
Scott J Hultgren
Michael G Caparon
Washington University in St. Louis · US

Funding

pan-Genome of E.coli in the bladder and gut of women with recurrent UTIP50DK064540 · NIDDK · WASHINGTON UNIVERSITY · PI HULTGREN, SCOTT J. · 2002 to 2017
$17.9M
Cytolysin-mediated translocation in S.pyogenes virulenceR01AI064721 · NIAID · WASHINGTON UNIVERSITY · PI CAPARON, MICHAEL G. · 2005 to 2014
$3.3M
NIAID NIH HHS AI064721NIAID NIH HHS R01 AI064721NIDDK NIH HHS DK064540NIDDK NIH HHS P50 DK064540
6 · The paper itself

Abstract

The Streptococcus pyogenes NAD-glycohydrolase (SPN) is a toxic enzyme that is introduced into infected host cells by the cytolysin-mediated translocation pathway. However, how S. pyogenes protects itself from the self-toxicity of SPN had been unknown. In this report, we describe immunity factor for SPN (IFS), a novel endogenous inhibitor that is essential for SPN expression. A small protein of 161 amino acids, IFS is localized in the bacterial cytoplasmic compartment. IFS forms a stable complex with SPN at a 1:1 molar ratio and inhibits SPN's NAD-glycohydrolase activity by acting as a competitive inhibitor of its beta-NAD+ substrate. Mutational studies revealed that the gene for IFS is essential for viability in those S. pyogenes strains that express an NAD-glycohydrolase activity. However, numerous strains contain a truncated allele of ifs that is linked to an NAD-glycohydrolase-deficient variant allele of spn. Of practical concern, IFS allowed the normally toxic SPN to be produced in the heterologous host Escherichia coli to facilitate its purification. To our knowledge, IFS is the first molecularly characterized endogenous inhibitor of a bacterial beta-NAD(+)-consuming toxin and may contribute protective functions in the streptococci to afford SPN-mediated pathogenesis.

Indexed as

Streptococcus pyogenesBacterial ProteinsEnzyme InhibitorsHumansMolecular Sequence DataNAD+ NucleosidaseSkinStreptococcal InfectionsBacterial ProteinsEnzyme InhibitorsNAD+ Nucleosidase

Identifiers

PMID16333395
PMCPMC1298937
OpenAlexW2147410828

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.