Evidence map›Paper›PMID 27188378›Full record

ArticleNature communications2016

Structural basis for haem piracy from host haemopexin by Haemophilus influenzae.

Silvia Zambolin, Bernard Clantin, Mohamed Chami, Sylviane Hoos, Ahmed Haouz, Vincent Villeret, Philippe Delepelaire

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Journal of bacteriology · 2022
    Article
  8. Article
  9. Article
  10. ECF Sigma Factor HxuI Is Critical forMicrobiology spectrum · 2022
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Metallotherapeutics development in the age of iron-clad bacteria.Metallomics : integrated biometal science · 2020
    Review
  16. Article
  17. Modeled Structure of the Cell Envelope Proteinase ofFrontiers in bioengineering and biotechnology · 2020
    Article
  18. Article
  19. The Role of Iron and Siderophores in Infection, and the Development of Siderophore Antibiotics.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2019
    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

7 authors at 2 institutions in 2 countries.

Silvia ZambolinCNRS, Université Paris 7 UMR 7099, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.
Bernard ClantinUniversité de Lille, CNRS, UMR 8576 - UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, Laboratoire de Biologie Structurale Intégrative, F 59000 Lille, France.
Mohamed ChamiCenter for Cellular Imaging and Nano Analytics (C-CINA), Biozentrum, University of Basel, Mattenstrasse 26, CH-4058 Basel, Switzerland.
Sylviane HoosInstitut Pasteur, Plate-forme de Biophysique, CNRS-UMR 3528, 25, rue du Dr Roux, 75724 Paris Cedex 15, France.
Ahmed HaouzInstitut Pasteur, Plate-forme de Cristallographie, CNRS-UMR 3528, 25, rue du Dr Roux, 75724 Paris Cedex 15, France.
Vincent VilleretUniversité de Lille, CNRS, UMR 8576 - UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, Laboratoire de Biologie Structurale Intégrative, F 59000 Lille, France.
Philippe DelepelaireCNRS, Université Paris 7 UMR 7099, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.ORCID 0000-0002-5190-7118
Centre National de la Recherche Scientifique · FRUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Haemophilus influenzae is an obligate human commensal/pathogen that requires haem for survival and can acquire it from several host haemoproteins, including haemopexin. The haem transport system from haem-haemopexin consists of HxuC, a haem receptor, and the two-partner-secretion system HxuB/HxuA. HxuA, which is exposed at the cell surface, is strictly required for haem acquisition from haemopexin. HxuA forms complexes with haem-haemopexin, leading to haem release and its capture by HxuC. The key question is how HxuA liberates haem from haemopexin. Here, we solve crystal structures of HxuA alone, and HxuA in complex with the N-terminal domain of haemopexin. A rational basis for the release of haem from haem-haemopexin is derived from both in vivo and in vitro studies. HxuA acts as a wedge that destabilizes the two-domains structure of haemopexin with a mobile loop on HxuA that favours haem ejection by redirecting key residues in the haem-binding pocket of haemopexin.

Indexed as

AnimalsBacterial ProteinsEscherichia coliHaemophilus influenzaeHemeMicroscopy, Electron, TransmissionMolecular StructureRabbitsReceptors, PeptideX-Ray DiffractionBacterial ProteinsHemehemopexin receptorReceptors, Peptide

Identifiers

PMID27188378
PMCPMC4873976
OpenAlexW2397483874

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.