Evidence map›Paper›PMID 41113855›Full record

ArticleFrontiers in molecular biosciences2025

Outer membrane vesicles from

Francesca Mensitieri, Federica Dell'Annunziata, Giulia Gaudino, Veronica Folliero, Gianluigi Franci, Fabrizio Dal Piaz, Viviana Izzo

Abstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2025. 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
–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

1 citing paper in PubMed.

  1. [Preparation of HLYVSPW peptide-displaying outer membrane vesicles and validation of their in vitro targeting effects on triple-negative breast cancer cells].Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2026
    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

7 authors.

Francesca Mensitieri *Department of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy.
Federica Dell'Annunziata *Department of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy.
Giulia GaudinoDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy.
Veronica FollieroDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy.
Gianluigi FranciDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy.
Fabrizio Dal PiazDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy.
Viviana IzzoDepartment of Medicine, Surgery and Dentistry "Scuola Medica Salernitana", University of Salerno, Baronissi, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Introduction: Anti-microbial peptides (AMPs) are a well-established alternative among antiviral and antibacterial agents, having considerable advantages over traditional antimicrobials in terms of biocompatibility and limited resistance development. However, a general poor bioavailability and short half-life limit their large-scale implementation. In this framework, different strategies are being explored, such as AMPs encapsulation or their functionalization on antigen-presenting platforms. In this work the evaluation of Methods: OMVs were engineered through the recombinant overexpression of an outer membrane chimeric protein, ClyA-AR23, obtained by combining Cytolysin A (ClyA) with the AR-23 antiviral peptide, derived from frog skin and active against herpes simplex viruses. LC-MS/MS was used to screen the presence of the recombinant protein in cells and OMVs. Plaque reduction assay after pre-incubation treatment and qPCR on viral transcript were used to evaluate ClyA-AR23 OMVs antiviral activity of the engineered vesicles. Results: The expression of ClyA-AR23 protein was verified in recombinant Discussion: In this work we provided a first evidence of AMPs functionalization on membrane vesicles of bacterial origin. The systems demonstrated to be active towards HSV-1 and HSV-2 viruses with negligible cytotoxicity on VERO-76 cells.

Indexed as

antimicrobial peptides (AMPs)antiviral activityAR-23chimeric proteinscytolysin A (ClyA)outer membrane vesicles (OMVs)presentation platforms

Identifiers

PMID41113855
PMCPMC12531040

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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.