Evidence map›Paper›PMID 23615912›Full record

ArticleThe Journal of biological chemistry2013

Ovalbumin-related protein X is a heparin-binding ov-serpin exhibiting antimicrobial activities.

Sophie Réhault-Godbert, Valérie Labas, Emmanuelle Helloin, Virginie Hervé-Grépinet, Cindy Slugocki, Magali Berges, Marie-Christine Bourin, Aurélien Brionne, Jean-Claude Poirier, Joël Gautron and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

22 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Effect of combined infection withOpen veterinary journal · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. The anti-bacterial iron-restriction defence mechanisms of egg white; the potential role of three lipocalin-like proteins in resistance against Salmonella.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2019
    Article
  14. Review
  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

12 authors at 5 institutions in 2 countries.

Sophie Réhault-GodbertInstitut National de la Recherche Agronomique, UR83 Recherches Avicoles, Fonction et Régulation des Protéines de l'Œuf, F-37380 Nouzilly, France. srehault@tours.inra.fr
Valérie Labas
Emmanuelle Helloin
Virginie Hervé-Grépinet
Cindy Slugocki
Magali Berges
Marie-Christine Bourin
Aurélien Brionne
Jean-Claude Poirier
Joël Gautron
Franck Coste
Yves Nys
Centre National de la Recherche Scientifique · FRInstitut National de la Recherche Agronomique · MAPhysiologie de la Reproduction et des Comportements · FRCentre de Biophysique Moléculaire · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ovalbumin family contains three proteins with high sequence similarity: ovalbumin, ovalbumin-related protein Y (OVAY), and ovalbumin-related protein X (OVAX). Ovalbumin is the major egg white protein with still undefined function, whereas the biological activity of OVAX and OVAY has not yet been explored. Similar to ovalbumin and OVAY, OVAX belongs to the ovalbumin serine protease inhibitor family (ov-serpin). We show that OVAX is specifically expressed by the magnum tissue, which is responsible for egg white formation. OVAX is also the main heparin-binding protein of egg white. This glycoprotein with a predicted reactive site at Lys(367)-His(368) is not able to inhibit trypsin, plasmin, or cathepsin G with or without heparin as a cofactor. Secondary structure of OVAX is similar to that of ovalbumin, but the three-dimensional model of OVAX reveals the presence of a cluster of exposed positive charges, which potentially explains the affinity of this ov-serpin for heparin, as opposed to ovalbumin. Interestingly, OVAX, unlike ovalbumin, displays antibacterial activities against both Listeria monocytogenes and Salmonella enterica sv. Enteritidis. These properties partly involve heparin-binding site(s) of the molecule as the presence of heparin reverses its anti-Salmonella but not its anti-Listeria potential. Altogether, these results suggest that OVAX and ovalbumin, although highly similar in sequence, have peculiar sequential and/or structural features that are likely to impact their respective biological functions.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsAnti-Bacterial AgentsAvian ProteinsBase SequenceCathepsin GChickensChromatography, AffinityFibrinolysinGlycosylationGram-Negative BacteriaGram-Positive BacteriaHeparinMicrobial Sensitivity TestsMolecular Sequence DataAnti-Bacterial AgentsAvian ProteinsCathepsin GFibrinolysinHeparinOvalbuminRNA, MessengerSerpinsTrypsin InhibitorsAntibacterial ProteinsChicken EggGlycoproteinHeparin Binding ProteinInnate ImmunityProtein StructureSerpin

Identifiers

PMID23615912
PMCPMC3682532
OpenAlexW1980740107

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.