Evidence map›Paper›PMID 41064820›Full record

ArticleVeterinary world2025

Multivalent display of VP28 on chimeric virus-like particles enhances binding to shrimp target tissues: A novel antiviral strategy against white spot syndrome virus.

Somkid Jaranathummakul, Pitchanee Jariyapong, Orawan Thongsum, Supawich Boonkua, Charoonroj Chotwiwatthanakun, Monsicha Somrit, Somluk Asuvapongpatana, Attaboon Wathammawut, Wattana Weerachatyanukul

Abstract read
In one paragraph

Article in Veterinary world, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Somkid JaranathummakulDepartment of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand.
Pitchanee JariyapongDepartment of Medical Science, School of Medicine, Walailak University, Thasala District, Nakhonsrithammarat, Thailand.
Orawan ThongsumDepartment of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand.
Supawich BoonkuaDepartment of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand.
Charoonroj ChotwiwatthanakunAcademic and Curriculum Division, Nakhonsawan Campus, Mahidol University, Nakhonsawan, Thailand.
Monsicha SomritDepartment of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand.
Somluk AsuvapongpatanaDepartment of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand.
Attaboon WathammawutDepartment of Anatomy, Faculty of Medicine, Sri Nakharinwiroj University, Bangkok, Thailand.
Wattana WeerachatyanukulDepartment of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background and Aim: White spot syndrome virus (WSSV) is a devastating pathogen in shrimp aquaculture, with viral protein 28 (VP28) playing a critical role in host cell attachment and entry. The extracellular domain of VP28 (residues 35-95) is immunogenic and essential for infection; however, its receptor interaction mechanisms remain incompletely elucidated. This study aimed to evaluate the tissue-binding affinity of full-length VP28 and its derived peptides (P1: Residues 35-65; P2: Residues 66-95) as well as a multimeric chimeric virus-like particle (K5-VLP) displaying VP28 on the surface of Materials and Methods: Recombinant VP28, synthetic peptides (P1, P2), and chimeric K5-VLP were produced and characterized. Binding and inhibition assays were performed using enzyme-linked immunosorbent assay and immunofluorescence microscopy on shrimp gill, hemocyte, muscle, stomach, and hepatopancreas tissues. Results: Full-length VP28 exhibited strong binding to gill, hemocyte, and muscle tissues. The P1 and P2 peptides showed moderate binding compared to rVP28. Notably, K5-VLP demonstrated a 1.7-fold higher binding affinity than rVP28 in gill tissues and significantly outperformed P1 and P2 peptides. Inhibition assays confirmed that K5-VLP more effectively interfered with VP28 binding than peptides. Structural analysis and transmission electron microscopy confirmed correct assembly and surface presentation of VP28 on the VLPs. Conclusion: Multimeric display of VP28 on K5-VLP enhances its binding affinity to shrimp tissues compared to monomeric or peptide forms. This suggests a promising platform for antiviral strategies, including competitive inhibition of WSSV entry and targeted therapeutic delivery in shrimp aquaculture.

Indexed as

aquaculture vaccinesMacrobrachium rosenbergii nodavirusshrimp immunitytissue bindingviral protein 28virus-like particleswhite spot syndrome virus

Identifiers

PMID41064820
PMCPMC12501573

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.