Evidence map›Paper›PMID 25311310›Full record

ArticleBioscience reports2014

Apo, Zn2+-bound and Mn2+-bound structures reveal ligand-binding properties of SitA from the pathogen Staphylococcus pseudintermedius.

Francesca Abate, Enrico Malito, Roberta Cozzi, Paola Lo Surdo, Domenico Maione, Matthew J Bottomley

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Structure and Function of the Zinc Binding Protein ZrgA fromInternational journal of molecular sciences · 2022
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Structure and Metal Binding Properties ofJournal of bacteriology · 2019
    Article
  8. Structures of the substrate-binding protein YfeA in apo and zinc-reconstituted holo forms.Acta crystallographica. Section D, Structural biology · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Protein Crystallography in Vaccine Research and Development.International journal of molecular sciences · 2015
    Review
  17. Manganese uptake and streptococcal virulence.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015
    Review
  18. Host-imposed manganese starvation of invading pathogens: two routes to the same destination.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015
    Review
  19. 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.

Francesca Abate*Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy.
Enrico Malito*Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy.
Roberta Cozzi*Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy.
Paola Lo Surdo*Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy.
Domenico Maione*Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy.
Matthew J Bottomley*Novartis Vaccines and Diagnostics srl, Via Fiorentina 1, 53100 Siena, Italy.
Novartis (Italy) · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Gram-positive bacterium Staphylococcus pseudintermedius is a leading cause of canine bacterial pyoderma, resulting in worldwide morbidity in dogs. S. pseudintermedius also causes life-threatening human infections. Furthermore, methicillin-resistant S. pseudintermedius is emerging, resembling the human health threat of methicillin-resistant Staphylococcus aureus. Therefore it is increasingly important to characterize targets for intervention strategies to counteract S. pseudintermedius infections. Here we used biophysical methods, mutagenesis, and X-ray crystallography, to define the ligand-binding properties and structure of SitA, an S. pseudintermedius surface lipoprotein. SitA was strongly and specifically stabilized by Mn2+ and Zn2+ ions. Crystal structures of SitA complexed with Mn2+ and Zn2+ revealed a canonical class III solute-binding protein with the metal cation bound in a cavity between N- and C-terminal lobes. Unexpectedly, one crystal contained both apo- and holo-forms of SitA, revealing a large side-chain reorientation of His64, and associated structural differences accompanying ligand binding. Such conformational changes may regulate fruitful engagement of the cognate ABC (ATP-binding cassette) transporter system (SitBC) required for metal uptake. These results provide the first detailed characterization and mechanistic insights for a potential therapeutic target of the major canine pathogen S. pseudintermedius, and also shed light on homologous structures in related staphylococcal pathogens afflicting humans.

Indexed as

Amino Acid SequenceAnimalsApolipoproteinsBacterial ProteinsCalorimetry, Differential ScanningCircular DichroismCrystallography, X-RayDog DiseasesDogsHumansManganeseModels, MolecularMolecular Sequence DataMutation, MissenseProtein BindingProtein MultimerizationApolipoproteinsBacterial ProteinsManganeseZinc

Identifiers

PMID25311310
PMCPMC4242081
OpenAlexW2090042352

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.