Evidence map›Paper›PMID 26969731›Full record

ArticleNucleic acids research2016

Structural characterization of the virulence factor Sda1 nuclease from Streptococcus pyogenes.

Andrea F Moon, Juno M Krahn, Xun Lu, Matthew J Cuneo, Lars C Pedersen

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
1.8field-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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.

  1. Neutrophil Extracellular Traps in Viral Infections.Pathogens (Basel, Switzerland) · 2025
    Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Immunomodulating Enzymes fromMicroorganisms · 2024
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Apurinic/apyrimidinic (AP) endonuclease 1 processing of AP sites with 5' mismatches.Acta crystallographica. Section D, Structural biology · 2018
    Article
  18. 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 3 institutions in 1 country.

Andrea F MoonGenome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA moon@niehs.nih.gov.
Juno M KrahnGenome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Xun LuSpallation Neutron Source, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.
Matthew J CuneoSpallation Neutron Source, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.
Lars C PedersenGenome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.
National Institute of Environmental Health Sciences · USOak Ridge National Laboratory · USNational Institutes of Health · US

Funding

Crystallographic studies of macromolecular structuresZIAES102645 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI PEDERSEN, LARS · 2009 to 2017
$9.4M
NIEHS NIH HHS ZIA ES102645
6 · The paper itself

Abstract

Infection by Group A Streptococcus pyogenes (GAS) is a leading cause of severe invasive disease in humans, including streptococcal toxic shock syndrome and necrotizing fasciitis. GAS infections lead to nearly 163,000 annual deaths worldwide. Hypervirulent strains of S. pyogenes have evolved a plethora of virulence factors that aid in disease-by promoting bacterial adhesion to host cells, subsequent invasion of deeper tissues and blocking the immune system's attempts to eradicate the infection. Expression and secretion of the extracellular nuclease Sda1 is advantageous for promoting bacterial dissemination throughout the host organism, and evasion of the host's innate immune response. Here we present two crystal structures of Sda1, as well as biochemical studies to address key structural features and surface residues involved in DNA binding and catalysis. In the active site, Asn211 is observed to directly chelate a hydrated divalent metal ion and Arg124, on the putative substrate binding loop, likely stabilizes the transition state during phosphodiester bond cleavage. These structures provide a foundation for rational drug design of small molecule inhibitors to be used in prevention of invasive streptococcal disease.

Indexed as

Bacterial ProteinsDeoxyribonuclease IModels, MolecularProtein DomainsProtein MultimerizationSequence AlignmentStreptococcus pyogenesVirulence FactorsBacterial ProteinsDeoxyribonuclease ISda1 protein, Streptococcus pyogenesVirulence Factors

Identifiers

PMID26969731
PMCPMC4856990
OpenAlexW2299401728

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.