Evidence map›Paper›PMID 39068414›Full record

ArticleBMC microbiology2024

Investigation of cross-opsonic effect leads to the discovery of PPIase-domain containing protein vaccine candidate to prevent infections by Gram-positive ESKAPE pathogens.

Océane Sadones, Eliza Kramarska, Diana Laverde, Rita Berisio, Johannes Huebner, Felipe Romero-Saavedra

Abstract read
In one paragraph

Article in BMC microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
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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

6 authors.

Océane SadonesDivision of pediatric infectious disease, Hauner children's hospital, LMU, Munich, Germany. sadonesoceane@gmail.com.
Eliza KramarskaInstitute of Biostructures and Bioimaging, Italian Research Council (CNR), Naples, Italy.
Diana LaverdeDivision of pediatric infectious disease, Hauner children's hospital, LMU, Munich, Germany.
Rita BerisioInstitute of Biostructures and Bioimaging, Italian Research Council (CNR), Naples, Italy.
Johannes HuebnerDivision of pediatric infectious disease, Hauner children's hospital, LMU, Munich, Germany. johannes.huebner@med.uni-muenchen.de.
Felipe Romero-SaavedraDivision of pediatric infectious disease, Hauner children's hospital, LMU, Munich, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundEnterococcus faecium and Staphylococcus aureus are the Gram-positive pathogens of the ESKAPE group, known to represent a great threat to human health due to their high virulence and multiple resistances to antibiotics. Combined, enterococci and S. aureus account for 26% of healthcare-associated infections and are the most common organisms responsible for blood stream infections. We previously showed that the peptidyl-prolyl cis/trans isomerase (PPIase) PpiC of E. faecium elicits the production of specific, opsonic, and protective antibodies that are effective against several strains of E. faecium and E. faecalis. Due to the ubiquitous characteristics of PPIases and their essential function within Gram-positive cells, we hypothesized a potential cross-reactive effect of anti-PpiC antibodies.

resultsOpsonophagocytic assays combined with bioinformatics led to the identification of the foldase protein PrsA as a new potential vaccine antigen in S. aureus. We show that PrsA is a stable dimeric protein able to elicit opsonic antibodies against the S. aureus strain MW2, as well as cross-binding and cross-opsonic in several S. aureus, E. faecium and E. faecalis strains.

conclusionsGiven the multiple antibiotic resistances S. aureus and enterococci present, finding preventive strategies is essential to fight those two nosocomial pathogens. The study shows the potential of PrsA as an antigen to use in vaccine formulation against the two dangerous Gram-positive ESKAPE bacteria. Our findings support the idea that PPIases should be further investigated as vaccine targets in the frame of pan-vaccinomics strategy.

Indexed as

Bacterial ProteinsEnterococcus faecalisEnterococcus faeciumPeptidylprolyl IsomeraseStaphylococcus aureusAnimalsAntibodies, BacterialAntigens, BacterialBacterial VaccinesCross ReactionsGram-Positive Bacterial InfectionsHumansMiceOpsonin ProteinsPhagocytosisStaphylococcal InfectionsAntibodies, BacterialAntigens, BacterialBacterial ProteinsBacterial VaccinesOpsonin ProteinsPeptidylprolyl IsomeraseAntigenCross-reactivityEnterococciESKAPE pathogensOpsonophagocytic assayPPIaseStaphylococcus aureusVaccines

Identifiers

PMID39068414
PMCPMC11282748

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Registered trials

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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.