Evidence map›Paper›PMID 26168161›Full record

ArticlePloS one2015

How Egg Case Proteins Can Protect Cuttlefish Offspring?

Valérie Cornet, Joël Henry, Didier Goux, Emilie Duval, Benoit Bernay, Gildas Le Corguillé, Erwan Corre, Céline Zatylny-Gaudin

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
7.5field-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

4 citing papers in PubMed, 19 citations in OpenAlex.

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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

8 authors at 4 institutions in 1 country.

Valérie CornetUniversité de Caen Basse-Normandie, F-14032, Caen, France; UMR 7208, BOREA CNRS INEE, F-14032, Caen, France.
Joël HenryUniversité de Caen Basse-Normandie, F-14032, Caen, France; UMR 7208, BOREA CNRS INEE, F-14032, Caen, France; Plateforme Post-génomique PROTEOGEN, F-14032, Caen, France.
Didier GouxUniversité de Caen Basse-Normandie, F-14032, Caen, France; CMAbio, F-14032, Caen, France.
Emilie DuvalUniversité de Caen Basse-Normandie, F-14032, Caen, France.
Benoit BernayUniversité de Caen Basse-Normandie, F-14032, Caen, France; Plateforme Post-génomique PROTEOGEN, F-14032, Caen, France.
Gildas Le CorguilléPlateforme ABiMS, Station biologique de Roscoff (UPMC-CNRS), F-29688, Roscoff, France.
Erwan CorrePlateforme ABiMS, Station biologique de Roscoff (UPMC-CNRS), F-29688, Roscoff, France.
Céline Zatylny-GaudinUniversité de Caen Basse-Normandie, F-14032, Caen, France; UMR 7208, BOREA CNRS INEE, F-14032, Caen, France.
Université de Caen Normandie · FRStation Biologique de Roscoff · FRBiologie des Organismes et Écosystèmes Aquatiques · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sepia officinalis egg protection is ensured by a complex capsule produced by the female accessory genital glands and the ink bag. Our study is focused on the proteins constituting the main egg case. De novo transcriptomes from female genital glands provided essential databases for protein identification. A proteomic approach in SDS-PAGE coupled with MS unveiled a new egg case protein family: SepECPs, for Sepia officinalis Egg Case Proteins. N-glycosylation was demonstrated by PAS staining SDS-PAGE gels. These glycoproteins are mainly produced in the main nidamental glands. SepECPs share high sequence homology, especially in the signal peptide and the three cysteine-rich domains. SepECPs have a high number of cysteines, with conserved motifs involved in 3D-structure. SDS-PAGE showed that SepECPs could form dimers; this result was confirmed by TEM observations, which also revealed a protein network. This network is similar to the capsule network, and it associates these structural proteins with polysaccharides, melanin and bacteria to form a tight mesh. Its hardness and elasticity provide physical protection to the embryo. In addition, SepECPs also have bacteriostatic antimicrobial activity on GRAM- bacteria. By observing the SepECP / Vibrio aestuarianus complex in SEM, we demonstrated the ability of these proteins to agglomerate bacteria and thus inhibit their growth. These original proteins identified from the outer egg case ensure the survival of the species by providing physical and chemical protection to the embryos released in the environment without any maternal protection.

Indexed as

OvumAnimalsDecapodiformesElectrophoresis, Polyacrylamide GelFemaleMicroscopy, Electron, ScanningMicroscopy, Electron, Transmission

Identifiers

PMID26168161
PMCPMC4500399
OpenAlexW2141151453

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.