Evidence map›Paper›PMID 34887426›Full record

ArticleScientific reports2021

Effect of human secretory calcium-binding phosphoprotein proline-glutamine rich 1 protein on Porphyromonas gingivalis and identification of its active portions.

Charline Mary, Aurélien Fouillen, Pierre Moffatt, Dainelys Guadarrama Bello, Rima M Wazen, Daniel Grenier, Antonio Nanci

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 48% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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 3 institutions in 1 country.

Charline MaryLaboratory for the Study of Calcified Tissues and Biomaterials, Faculty of Dental Medicine, Université de Montréal, Montréal, Québec, H3T 1J4, Canada.
Aurélien FouillenLaboratory for the Study of Calcified Tissues and Biomaterials, Faculty of Dental Medicine, Université de Montréal, Montréal, Québec, H3T 1J4, Canada.
Pierre MoffattDepartment of Human Genetics, McGill University, Montreal, Québec, H3A 0G4, Canada.
Dainelys Guadarrama BelloLaboratory for the Study of Calcified Tissues and Biomaterials, Faculty of Dental Medicine, Université de Montréal, Montréal, Québec, H3T 1J4, Canada.
Rima M WazenLaboratory for the Study of Calcified Tissues and Biomaterials, Faculty of Dental Medicine, Université de Montréal, Montréal, Québec, H3T 1J4, Canada.
Daniel GrenierOral Ecology Research Group, Faculty of Dental Medicine, Université Laval, Québec, Québec, G1V 0A6, Canada.
Antonio NanciLaboratory for the Study of Calcified Tissues and Biomaterials, Faculty of Dental Medicine, Université de Montréal, Montréal, Québec, H3T 1J4, Canada. antonio.nanci@umontreal.ca.
Université de Montréal · CAShriners Hospitals for Children - Canada · CAUniversité Laval · CA

Funding

CIHR MOP-110972
6 · The paper itself

Abstract

The mouth environment comprises the second most significant microbiome in the body, and its equilibrium is critical in oral health. Secretory calcium-binding phosphoprotein proline-glutamine rich 1 (SCPPPQ1), a protein normally produced by the gingival epithelium to mediate its attachment to teeth, was suggested to be bactericidal. Our aim was to further explore the antibacterial potential of human SCPPPQ1 by characterizing its mode of action and identifying its active portions. In silico analysis showed that it has molecular parallels with antimicrobial peptides. Incubation of Porphyromonas gingivalis, a major periodontopathogen, with the full-length protein resulted in decrease in bacterial number, formation of aggregates and membrane disruptions. Analysis of SCPPPQ1-derived peptides indicated that these effects are sustained by specific regions of the molecule. Altogether, these data suggest that human SCPPPQ1 exhibits antibacterial capacity and provide new insight into its mechanism of action.

Indexed as

Amino Acid SequenceAntimicrobial PeptidesCalcium-Binding ProteinsDisease ResistanceHost-Pathogen InteractionsHumansMicrobial Sensitivity TestsModels, MolecularPhosphoproteinsPorphyromonas gingivalisProtein BindingProtein ConformationStructure-Activity RelationshipAntimicrobial PeptidesCalcium-Binding ProteinsPhosphoproteins

Identifiers

PMID34887426
PMCPMC8660882
OpenAlexW4200077497

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.