Evidence map›Paper›PMID 41746052›Full record

ArticleVaccines2026

EPIclip: A Novel Approach for the Production of Decorated Virus-Like Particles Mediated by High-Affinity Protein Binding Partners.

Aleksandra Moleda, Olivia Bagshaw, Jonas Repkewitz, Suaad Ahmed, Attila Jakab, Pamela Gomez Jordan, Sherin Sunny, Jean-Christophe Bourdon, John Foerster

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Article in Vaccines, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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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

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

9 authors.

Aleksandra MoledaScancell Ltd., Oxford OX4 4GD, UK.
Olivia BagshawGlen Clova Scientific Ltd., Dundee G2 4JR, UK.
Jonas RepkewitzKing's College Hospital NHS Foundation Trust, London SE5 9RS, UK.ORCID 0009-0006-9191-2129
Suaad AhmedGlen Clova Scientific Ltd., Dundee G2 4JR, UK.
Attila JakabGlen Clova Scientific Ltd., Dundee G2 4JR, UK.
Pamela Gomez JordanGlen Clova Scientific Ltd., Dundee G2 4JR, UK.
Sherin SunnyGlen Clova Scientific Ltd., Dundee G2 4JR, UK.
Jean-Christophe BourdonSchool of Medicine, University of Dundee, Dundee DD1 9SY, UK.ORCID 0000-0003-4623-9386
John FoersterGlen Clova Scientific Ltd., Dundee G2 4JR, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundVirus-like particles (VLPs) represent key tools for the development of vaccines due to their ability to induce a potent immune response to epitopes presented on their surface. However, the decoration of VLPs with a complete heterologous protein on the surface remains a bottleneck for clinical translation due to the complexity of manufacture. We present a novel platform, EPIclip™, for the decoration of VLPs mediated by high-affinity protein binding partners, colicin E7 (ColE7) and immunity protein 7 (Im7), within a single prokaryotic host. We evaluate this approach using a modified hepatitis B core capsid protein and IL-31 as a model epitope. IL-31 is a prominent therapeutic target for the development of pruritic diseases.

methodsWe explore the design and development of the platform, including the use of T-cell-stimulating peptides. We demonstrate several small-scale purification methods for the candidate VLP, as well as morphological analysis by transmission electron microscopy (TEM). Further, we vaccinate mice with IL-31-displaying VLPs to evaluate immunogenicity and the ability to prevent IL-31-induced pruritus in vivo.

resultsOur results demonstrate that decorated VLPs dosed in mice elicit an IgG response against IL-31 with at least six months of durability. In addition, IL-31-displaying VLPs suppress the development of IL-31-induced pruritus, confirming in vivo target neutralisation. Notably, IL-31-displaying VLPs induce a strong T-cell response against the VLP capsid but not against the cytokine, confirming a B-cell-biased immune response and the absence of detrimental autoreactive T cells. We further demonstrate the translation of this system with an additional virus capsid: tomato aspermy virus (TAV).

conclusionsTaken together, the novel EPIclip™ platform may represent a promising therapeutic approach for pruritic diseases. Additionally, this modular system could be adapted for a wide range of research as well as human and veterinary therapeutic applications.

Indexed as

expression systeminterleukin-31vaccine developmentvirus-like particles

Identifiers

PMID41746052
PMCPMC12945302

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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.