Evidence map›Paper›PMID 19053425›Full record

ArticleJournal of the American Chemical Society2008

The role of electrostatics in siderophore recognition by the immunoprotein Siderocalin.

Trisha M Hoette, Rebecca J Abergel, Jide Xu, Roland K Strong, Kenneth N Raymond

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

23 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Iron Acquisition by Bacterial Pathogens: Beyond Tris-Catecholate Complexes.Chembiochem : a European journal of chemical biology · 2020
    Review
  3. Article
  4. Article
  5. Article
  6. Lipocalin 2 alleviates iron toxicity by facilitating hypoferremia of inflammation and limiting catalytic iron generation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2016
    Article
  7. Coordination Chemistry of Microbial Iron Transport.Accounts of chemical research · 2015
    Article
  8. Article
  9. EGCG inhibit chemical reactivity of iron through forming an Ngal-EGCG-iron complex.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2013
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. The v-myc-induced Q83 lipocalin is a siderocalin.The Journal of biological chemistry · 2010
    Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

Trisha M HoetteDepartment of Chemistry, University of California, Berkeley, California 94720-1460, USA.
Rebecca J Abergel
Jide Xu
Roland K Strong
Kenneth N Raymond
University of California, Berkeley · US

Funding

Coordination Chemistry of Microbial Iron Transport CompoundsR01AI011744 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI RAYMOND, KENNETH N · 1986 to 2013
$4.1M
NIAID NIH HHS AI117448NIAID NIH HHS R01 AI011744
6 · The paper itself

Abstract

Iron is required for virulence of most bacterial pathogens, many of which rely on siderophores, small-molecule chelators, to scavenge iron in mammalian hosts. As an immune response, the human protein Siderocalin binds both apo and ferric siderophores in order to intercept delivery of iron to the bacterium, impeding virulence. The introduction of steric clashes into the siderophore structure is an important mechanism of evading sequestration. However, in the absence of steric incompatibilities, electrostatic interactions determine siderophore strength of binding by Siderocalin. By using a series of isosteric enterobactin analogues, the contribution of electrostatic interactions, including both charge-charge and cation-pi, to the recognition of 2,3-catecholate siderophores has been deconvoluted. The analogues used in the study incorporate a systematic combination of 2,3-catecholamide (CAM) and N-hydroxypyridinonate (1,2-HOPO) binding units on a tris(2-aminoethyl)amine (tren) backbone, [tren(CAM)(m)(1,2-HOPO)(n), where m = 0, 1, 2, or 3 and n = 3 - m]. The shape complementarity of the synthetic analogue series was determined through small-molecule crystallography, and the binding interactions were investigated through a fluorescence-based binding assay. These results were modeled and correlated through ab initio calculations of the electrostatic properties of the binding units. Although all the analogues are accommodated in the binding pocket of Siderocalin, the ferric complexes incorporating decreasing numbers of CAM units are bound with decreasing affinities (K(d) = >600, 43, 0.8, and 0.3 nM for m = 0-3). These results elucidate the role of electrostatics in the mechanism of siderophore recognition by Siderocalin.

Indexed as

AnimalsBinding SitesCrystallography, X-RayDihydropyridinesEnterobactinHumansImmunoproteinsIronIron Chelating AgentsKineticsLigandsMolecular ConformationSiderophoresSoftwareStatic ElectricitySubstrate SpecificityDihydropyridinesEnterobactinImmunoproteinsIronIron Chelating AgentsLigandsSiderophores

Identifiers

PMID19053425
PMCPMC2778733
OpenAlexW2044434077

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.